HEADER HYDROLASE 16-DEC-16 5MPA
TITLE 26S PROTEASOME IN PRESENCE OF ATP (S2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 3 CHAIN: a, A;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA,MULTICATALYTIC ENDOPEPTIDASE
COMPND 5 COMPLEX C7,PROTEASOME COMPONENT C7-ALPHA,PROTEASOME COMPONENT Y8,
COMPND 6 PROTEINASE YSCE SUBUNIT 7,SCL1 SUPPRESSOR PROTEIN;
COMPND 7 EC: 3.4.25.1;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 10 CHAIN: b, B;
COMPND 11 SYNONYM: MACROPAIN SUBUNIT Y7,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 12 SUBUNIT Y7,PROTEASOME COMPONENT Y7,PROTEINASE YSCE SUBUNIT 7;
COMPND 13 EC: 3.4.25.1;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 16 CHAIN: c, C;
COMPND 17 SYNONYM: MACROPAIN SUBUNIT Y13,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 18 SUBUNIT Y13,PROTEASOME COMPONENT Y13,PROTEINASE YSCE SUBUNIT 13;
COMPND 19 EC: 3.4.25.1;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 22 CHAIN: d, D;
COMPND 23 SYNONYM: MACROPAIN SUBUNIT PRE6,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 24 SUBUNIT PRE6,PROTEASOME COMPONENT PRE6,PROTEINASE YSCE SUBUNIT PRE6;
COMPND 25 EC: 3.4.25.1;
COMPND 26 MOL_ID: 5;
COMPND 27 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 28 CHAIN: e, E;
COMPND 29 SYNONYM: MACROPAIN SUBUNIT PUP2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 30 SUBUNIT PUP2,PROTEASOME COMPONENT PUP2,PROTEINASE YSCE SUBUNIT PUP2;
COMPND 31 EC: 3.4.25.1;
COMPND 32 MOL_ID: 6;
COMPND 33 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 34 CHAIN: f, F;
COMPND 35 SYNONYM: MACROPAIN SUBUNIT PRE5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 36 SUBUNIT PRE5,PROTEASOME COMPONENT PRE5,PROTEINASE YSCE SUBUNIT PRE5;
COMPND 37 EC: 3.4.25.1;
COMPND 38 MOL_ID: 7;
COMPND 39 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 40 CHAIN: g, G;
COMPND 41 SYNONYM: MACROPAIN SUBUNIT C1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 42 SUBUNIT C1,PROTEASOME COMPONENT C1,PROTEINASE YSCE SUBUNIT 1;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 46 CHAIN: h, 1;
COMPND 47 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 48 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 49 EC: 3.4.25.1;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 52 CHAIN: i, 2;
COMPND 53 SYNONYM: MACROPAIN SUBUNIT PUP1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 54 SUBUNIT PUP1,PROTEASOME COMPONENT PUP1,PROTEINASE YSCE SUBUNIT PUP1;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 58 CHAIN: j, 3;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 60 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 64 CHAIN: k, 4;
COMPND 65 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 66 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;
COMPND 67 EC: 3.4.25.1;
COMPND 68 MOL_ID: 12;
COMPND 69 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 70 CHAIN: l, 5;
COMPND 71 SYNONYM: MACROPAIN SUBUNIT PRE2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 72 SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,PROTEINASE YSCE SUBUNIT PRE2;
COMPND 73 EC: 3.4.25.1;
COMPND 74 MOL_ID: 13;
COMPND 75 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 76 CHAIN: m, 6;
COMPND 77 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 78 COMPONENT C5;
COMPND 79 EC: 3.4.25.1;
COMPND 80 MOL_ID: 14;
COMPND 81 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 82 CHAIN: n, 7;
COMPND 83 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 84 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 85 EC: 3.4.25.1;
COMPND 86 MOL_ID: 15;
COMPND 87 MOLECULE: 26S PROTEASE REGULATORY SUBUNIT 7 HOMOLOG;
COMPND 88 CHAIN: H;
COMPND 89 SYNONYM: PROTEIN CIM5,TAT-BINDING HOMOLOG 3;
COMPND 90 MOL_ID: 16;
COMPND 91 MOLECULE: 26S PROTEASE REGULATORY SUBUNIT 4 HOMOLOG;
COMPND 92 CHAIN: I;
COMPND 93 SYNONYM: TAT-BINDING HOMOLOG 5;
COMPND 94 MOL_ID: 17;
COMPND 95 MOLECULE: 26S PROTEASE REGULATORY SUBUNIT 6B HOMOLOG;
COMPND 96 CHAIN: K;
COMPND 97 SYNONYM: PROTEIN YNT1,TAT-BINDING HOMOLOG 2;
COMPND 98 MOL_ID: 18;
COMPND 99 MOLECULE: 26S PROTEASE SUBUNIT RPT4;
COMPND 100 CHAIN: L;
COMPND 101 SYNONYM: 26S PROTEASE SUBUNIT SUG2,PROTEASOMAL CAP SUBUNIT;
COMPND 102 MOL_ID: 19;
COMPND 103 MOLECULE: 26S PROTEASE REGULATORY SUBUNIT 6A;
COMPND 104 CHAIN: M;
COMPND 105 SYNONYM: TAT-BINDING PROTEIN HOMOLOG 1,TBP-1;
COMPND 106 MOL_ID: 20;
COMPND 107 MOLECULE: 26S PROTEASE REGULATORY SUBUNIT 8 HOMOLOG;
COMPND 108 CHAIN: J;
COMPND 109 SYNONYM: PROTEIN CIM3,PROTEIN SUG1,TAT-BINDING PROTEIN TBY1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 8 S288C);
SOURCE 9 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 10 ORGANISM_TAXID: 559292;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 13 S288C);
SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 15 ORGANISM_TAXID: 559292;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 18 S288C);
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 559292;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 23 S288C);
SOURCE 24 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 25 ORGANISM_TAXID: 559292;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 28 S288C);
SOURCE 29 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 30 ORGANISM_TAXID: 559292;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 33 S288C);
SOURCE 34 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 35 ORGANISM_TAXID: 559292;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 38 S288C);
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 559292;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 43 S288C);
SOURCE 44 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 45 ORGANISM_TAXID: 559292;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 48 S288C);
SOURCE 49 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 50 ORGANISM_TAXID: 559292;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 53 S288C);
SOURCE 54 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 55 ORGANISM_TAXID: 559292;
SOURCE 56 MOL_ID: 12;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 58 S288C);
SOURCE 59 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 60 ORGANISM_TAXID: 559292;
SOURCE 61 MOL_ID: 13;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 63 S288C);
SOURCE 64 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 65 ORGANISM_TAXID: 559292;
SOURCE 66 MOL_ID: 14;
SOURCE 67 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 68 S288C);
SOURCE 69 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 70 ORGANISM_TAXID: 559292;
SOURCE 71 MOL_ID: 15;
SOURCE 72 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 73 S288C);
SOURCE 74 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 75 ORGANISM_TAXID: 559292;
SOURCE 76 MOL_ID: 16;
SOURCE 77 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 78 S288C);
SOURCE 79 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 80 ORGANISM_TAXID: 559292;
SOURCE 81 MOL_ID: 17;
SOURCE 82 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 83 S288C);
SOURCE 84 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 85 ORGANISM_TAXID: 559292;
SOURCE 86 MOL_ID: 18;
SOURCE 87 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 88 S288C);
SOURCE 89 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 90 ORGANISM_TAXID: 559292;
SOURCE 91 MOL_ID: 19;
SOURCE 92 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 93 S288C);
SOURCE 94 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 95 ORGANISM_TAXID: 559292;
SOURCE 96 MOL_ID: 20;
SOURCE 97 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 98 S288C);
SOURCE 99 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 100 ORGANISM_TAXID: 559292
KEYWDS MACROMOLECULAR COMPLEX, 26S PROTEASOME, PROTEASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.WEHMER,T.RUDACK,F.BECK,A.AUFDERHEIDE,G.PFEIFER,J.M.PLITZKO,
AUTHOR 2 F.FOERSTER,K.SCHULTEN,W.BAUMEISTER,E.SAKATA
REVDAT 2 02-AUG-17 5MPA 1
REVDAT 1 08-MAR-17 5MPA 0
JRNL AUTH M.WEHMER,T.RUDACK,F.BECK,A.AUFDERHEIDE,G.PFEIFER,
JRNL AUTH 2 J.M.PLITZKO,F.FORSTER,K.SCHULTEN,W.BAUMEISTER,E.SAKATA
JRNL TITL STRUCTURAL INSIGHTS INTO THE FUNCTIONAL CYCLE OF THE ATPASE
JRNL TITL 2 MODULE OF THE 26S PROTEASOME.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 1305 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28115689
JRNL DOI 10.1073/PNAS.1621129114
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : TOM TOOLBOX, TOM2, CTFFIND, MDFF,
REMARK 3 RELION, RELION, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.500
REMARK 3 NUMBER OF PARTICLES : 193337
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5MPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002774.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : 26S PROTEASOME OF SACCHAROMYCES
REMARK 245 CEREVISIAE IN PRESENCE OF ATP
REMARK 245 (S2)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 45.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 34-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, d, e, f, g, h, i, j,
REMARK 350 AND CHAINS: k, l, m, n, A, B, C, D, E,
REMARK 350 AND CHAINS: F, G, 1, 2, 3, 4, 5, 6, 7, H,
REMARK 350 AND CHAINS: I, K, L, M, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET a -8
REMARK 465 SER a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 ALA a -4
REMARK 465 ALA a -3
REMARK 465 ALA a -2
REMARK 465 SER a -1
REMARK 465 ALA a 0
REMARK 465 ALA a 1
REMARK 465 ASP a 243
REMARK 465 MET c 0
REMARK 465 LYS c 245
REMARK 465 LYS c 246
REMARK 465 ASP c 247
REMARK 465 GLU c 248
REMARK 465 ASP c 249
REMARK 465 GLU c 250
REMARK 465 GLU c 251
REMARK 465 ALA c 252
REMARK 465 ASP c 253
REMARK 465 GLU c 254
REMARK 465 ASP c 255
REMARK 465 MET c 256
REMARK 465 LYS c 257
REMARK 465 MET d -1
REMARK 465 SER d 0
REMARK 465 GLN d 241
REMARK 465 GLN d 242
REMARK 465 GLU d 243
REMARK 465 GLN d 244
REMARK 465 ASP d 245
REMARK 465 LYS d 246
REMARK 465 LYS d 247
REMARK 465 LYS d 248
REMARK 465 LYS d 249
REMARK 465 SER d 250
REMARK 465 ASN d 251
REMARK 465 HIS d 252
REMARK 465 MET e -7
REMARK 465 PHE e -6
REMARK 465 LEU e -5
REMARK 465 THR e -4
REMARK 465 ARG e -3
REMARK 465 SER e -2
REMARK 465 GLU e -1
REMARK 465 TYR e 0
REMARK 465 SER e 243
REMARK 465 PRO e 244
REMARK 465 GLU e 245
REMARK 465 GLU e 246
REMARK 465 ALA e 247
REMARK 465 ASP e 248
REMARK 465 VAL e 249
REMARK 465 GLU e 250
REMARK 465 MET e 251
REMARK 465 SER e 252
REMARK 465 MET f 0
REMARK 465 PHE f 1
REMARK 465 ARG f 2
REMARK 465 MET g -3
REMARK 465 THR g -2
REMARK 465 SER g -1
REMARK 465 ILE g 0
REMARK 465 GLY g 1
REMARK 465 GLY g 245
REMARK 465 ASP g 246
REMARK 465 ASP g 247
REMARK 465 ASP g 248
REMARK 465 GLU g 249
REMARK 465 ASP g 250
REMARK 465 GLU g 251
REMARK 465 ASP g 252
REMARK 465 ASP g 253
REMARK 465 SER g 254
REMARK 465 ASP g 255
REMARK 465 ASN g 256
REMARK 465 VAL g 257
REMARK 465 MET g 258
REMARK 465 SER g 259
REMARK 465 SER g 260
REMARK 465 ASP g 261
REMARK 465 ASP g 262
REMARK 465 GLU g 263
REMARK 465 ASN g 264
REMARK 465 ALA g 265
REMARK 465 PRO g 266
REMARK 465 VAL g 267
REMARK 465 ALA g 268
REMARK 465 THR g 269
REMARK 465 ASN g 270
REMARK 465 ALA g 271
REMARK 465 ASN g 272
REMARK 465 ALA g 273
REMARK 465 THR g 274
REMARK 465 THR g 275
REMARK 465 ASP g 276
REMARK 465 GLN g 277
REMARK 465 GLU g 278
REMARK 465 GLY g 279
REMARK 465 ASP g 280
REMARK 465 ILE g 281
REMARK 465 HIS g 282
REMARK 465 LEU g 283
REMARK 465 GLU g 284
REMARK 465 MET h -18
REMARK 465 ASN h -17
REMARK 465 GLY h -16
REMARK 465 ILE h -15
REMARK 465 GLN h -14
REMARK 465 VAL h -13
REMARK 465 ASP h -12
REMARK 465 ILE h -11
REMARK 465 ASN h -10
REMARK 465 ARG h -9
REMARK 465 LEU h -8
REMARK 465 LYS h -7
REMARK 465 LYS h -6
REMARK 465 GLY h -5
REMARK 465 GLU h -4
REMARK 465 VAL h -3
REMARK 465 SER h -2
REMARK 465 LEU h -1
REMARK 465 GLY h 0
REMARK 465 MET i -28
REMARK 465 ALA i -27
REMARK 465 GLY i -26
REMARK 465 LEU i -25
REMARK 465 SER i -24
REMARK 465 PHE i -23
REMARK 465 ASP i -22
REMARK 465 ASN i -21
REMARK 465 TYR i -20
REMARK 465 GLN i -19
REMARK 465 ARG i -18
REMARK 465 ASN i -17
REMARK 465 ASN i -16
REMARK 465 PHE i -15
REMARK 465 LEU i -14
REMARK 465 ALA i -13
REMARK 465 GLU i -12
REMARK 465 ASN i -11
REMARK 465 SER i -10
REMARK 465 HIS i -9
REMARK 465 THR i -8
REMARK 465 GLN i -7
REMARK 465 PRO i -6
REMARK 465 LYS i -5
REMARK 465 ALA i -4
REMARK 465 THR i -3
REMARK 465 SER i -2
REMARK 465 THR i -1
REMARK 465 GLY i 0
REMARK 465 GLN i 227
REMARK 465 VAL i 228
REMARK 465 ASP i 229
REMARK 465 ILE i 230
REMARK 465 THR i 231
REMARK 465 ALA i 232
REMARK 465 MET j 0
REMARK 465 GLN k 196
REMARK 465 ALA k 197
REMARK 465 GLN k 198
REMARK 465 MET l -74
REMARK 465 GLN l -73
REMARK 465 ALA l -72
REMARK 465 ILE l -71
REMARK 465 ALA l -70
REMARK 465 ASP l -69
REMARK 465 SER l -68
REMARK 465 PHE l -67
REMARK 465 SER l -66
REMARK 465 VAL l -65
REMARK 465 PRO l -64
REMARK 465 ASN l -63
REMARK 465 ARG l -62
REMARK 465 LEU l -61
REMARK 465 VAL l -60
REMARK 465 LYS l -59
REMARK 465 GLU l -58
REMARK 465 LEU l -57
REMARK 465 GLN l -56
REMARK 465 TYR l -55
REMARK 465 ASP l -54
REMARK 465 ASN l -53
REMARK 465 GLU l -52
REMARK 465 GLN l -51
REMARK 465 ASN l -50
REMARK 465 LEU l -49
REMARK 465 GLU l -48
REMARK 465 SER l -47
REMARK 465 ASP l -46
REMARK 465 PHE l -45
REMARK 465 VAL l -44
REMARK 465 THR l -43
REMARK 465 GLY l -42
REMARK 465 ALA l -41
REMARK 465 SER l -40
REMARK 465 GLN l -39
REMARK 465 PHE l -38
REMARK 465 GLN l -37
REMARK 465 ARG l -36
REMARK 465 LEU l -35
REMARK 465 ALA l -34
REMARK 465 PRO l -33
REMARK 465 SER l -32
REMARK 465 LEU l -31
REMARK 465 THR l -30
REMARK 465 VAL l -29
REMARK 465 PRO l -28
REMARK 465 PRO l -27
REMARK 465 ILE l -26
REMARK 465 ALA l -25
REMARK 465 SER l -24
REMARK 465 PRO l -23
REMARK 465 GLN l -22
REMARK 465 GLN l -21
REMARK 465 PHE l -20
REMARK 465 LEU l -19
REMARK 465 ARG l -18
REMARK 465 ALA l -17
REMARK 465 HIS l -16
REMARK 465 THR l -15
REMARK 465 ASP l -14
REMARK 465 ASP l -13
REMARK 465 SER l -12
REMARK 465 ARG l -11
REMARK 465 ASN l -10
REMARK 465 PRO l -9
REMARK 465 ASP l -8
REMARK 465 CYS l -7
REMARK 465 LYS l -6
REMARK 465 ILE l -5
REMARK 465 LYS l -4
REMARK 465 ILE l -3
REMARK 465 ALA l -2
REMARK 465 HIS l -1
REMARK 465 GLY l 0
REMARK 465 MET m -18
REMARK 465 ALA m -17
REMARK 465 THR m -16
REMARK 465 ILE m -15
REMARK 465 ALA m -14
REMARK 465 SER m -13
REMARK 465 GLU m -12
REMARK 465 TYR m -11
REMARK 465 SER m -10
REMARK 465 SER m -9
REMARK 465 GLU m -8
REMARK 465 ALA m -7
REMARK 465 SER m -6
REMARK 465 ASN m -5
REMARK 465 THR m -4
REMARK 465 PRO m -3
REMARK 465 ILE m -2
REMARK 465 GLU m -1
REMARK 465 HIS m 0
REMARK 465 MET n -32
REMARK 465 ASN n -31
REMARK 465 HIS n -30
REMARK 465 ASP n -29
REMARK 465 PRO n -28
REMARK 465 PHE n -27
REMARK 465 SER n -26
REMARK 465 TRP n -25
REMARK 465 GLY n -24
REMARK 465 ARG n -23
REMARK 465 PRO n -22
REMARK 465 ALA n -21
REMARK 465 ASP n -20
REMARK 465 SER n -19
REMARK 465 THR n -18
REMARK 465 TYR n -17
REMARK 465 GLY n -16
REMARK 465 ALA n -15
REMARK 465 TYR n -14
REMARK 465 ASN n -13
REMARK 465 THR n -12
REMARK 465 GLN n -11
REMARK 465 ILE n -10
REMARK 465 ALA n -9
REMARK 465 ASN n -8
REMARK 465 ALA n -7
REMARK 465 GLY n -6
REMARK 465 ALA n -5
REMARK 465 SER n -4
REMARK 465 PRO n -3
REMARK 465 MET n -2
REMARK 465 VAL n -1
REMARK 465 ASN n 0
REMARK 465 ILE n 233
REMARK 465 MET A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 ALA A -5
REMARK 465 ALA A -4
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 SER A -1
REMARK 465 ALA A 0
REMARK 465 ALA A 1
REMARK 465 ASP A 243
REMARK 465 MET C 0
REMARK 465 LYS C 245
REMARK 465 LYS C 246
REMARK 465 ASP C 247
REMARK 465 GLU C 248
REMARK 465 ASP C 249
REMARK 465 GLU C 250
REMARK 465 GLU C 251
REMARK 465 ALA C 252
REMARK 465 ASP C 253
REMARK 465 GLU C 254
REMARK 465 ASP C 255
REMARK 465 MET C 256
REMARK 465 LYS C 257
REMARK 465 MET D -1
REMARK 465 SER D 0
REMARK 465 GLN D 241
REMARK 465 GLN D 242
REMARK 465 GLU D 243
REMARK 465 GLN D 244
REMARK 465 ASP D 245
REMARK 465 LYS D 246
REMARK 465 LYS D 247
REMARK 465 LYS D 248
REMARK 465 LYS D 249
REMARK 465 SER D 250
REMARK 465 ASN D 251
REMARK 465 HIS D 252
REMARK 465 MET E -7
REMARK 465 PHE E -6
REMARK 465 LEU E -5
REMARK 465 THR E -4
REMARK 465 ARG E -3
REMARK 465 SER E -2
REMARK 465 GLU E -1
REMARK 465 TYR E 0
REMARK 465 SER E 243
REMARK 465 PRO E 244
REMARK 465 GLU E 245
REMARK 465 GLU E 246
REMARK 465 ALA E 247
REMARK 465 ASP E 248
REMARK 465 VAL E 249
REMARK 465 GLU E 250
REMARK 465 MET E 251
REMARK 465 SER E 252
REMARK 465 MET F 0
REMARK 465 MET G -3
REMARK 465 THR G -2
REMARK 465 SER G -1
REMARK 465 ILE G 0
REMARK 465 GLY G 1
REMARK 465 GLY G 245
REMARK 465 ASP G 246
REMARK 465 ASP G 247
REMARK 465 ASP G 248
REMARK 465 GLU G 249
REMARK 465 ASP G 250
REMARK 465 GLU G 251
REMARK 465 ASP G 252
REMARK 465 ASP G 253
REMARK 465 SER G 254
REMARK 465 ASP G 255
REMARK 465 ASN G 256
REMARK 465 VAL G 257
REMARK 465 MET G 258
REMARK 465 SER G 259
REMARK 465 SER G 260
REMARK 465 ASP G 261
REMARK 465 ASP G 262
REMARK 465 GLU G 263
REMARK 465 ASN G 264
REMARK 465 ALA G 265
REMARK 465 PRO G 266
REMARK 465 VAL G 267
REMARK 465 ALA G 268
REMARK 465 THR G 269
REMARK 465 ASN G 270
REMARK 465 ALA G 271
REMARK 465 ASN G 272
REMARK 465 ALA G 273
REMARK 465 THR G 274
REMARK 465 THR G 275
REMARK 465 ASP G 276
REMARK 465 GLN G 277
REMARK 465 GLU G 278
REMARK 465 GLY G 279
REMARK 465 ASP G 280
REMARK 465 ILE G 281
REMARK 465 HIS G 282
REMARK 465 LEU G 283
REMARK 465 GLU G 284
REMARK 465 MET 1 -18
REMARK 465 ASN 1 -17
REMARK 465 GLY 1 -16
REMARK 465 ILE 1 -15
REMARK 465 GLN 1 -14
REMARK 465 VAL 1 -13
REMARK 465 ASP 1 -12
REMARK 465 ILE 1 -11
REMARK 465 ASN 1 -10
REMARK 465 ARG 1 -9
REMARK 465 LEU 1 -8
REMARK 465 LYS 1 -7
REMARK 465 LYS 1 -6
REMARK 465 GLY 1 -5
REMARK 465 GLU 1 -4
REMARK 465 VAL 1 -3
REMARK 465 SER 1 -2
REMARK 465 LEU 1 -1
REMARK 465 GLY 1 0
REMARK 465 MET 2 -28
REMARK 465 ALA 2 -27
REMARK 465 GLY 2 -26
REMARK 465 LEU 2 -25
REMARK 465 SER 2 -24
REMARK 465 PHE 2 -23
REMARK 465 ASP 2 -22
REMARK 465 ASN 2 -21
REMARK 465 TYR 2 -20
REMARK 465 GLN 2 -19
REMARK 465 ARG 2 -18
REMARK 465 ASN 2 -17
REMARK 465 ASN 2 -16
REMARK 465 PHE 2 -15
REMARK 465 LEU 2 -14
REMARK 465 ALA 2 -13
REMARK 465 GLU 2 -12
REMARK 465 ASN 2 -11
REMARK 465 SER 2 -10
REMARK 465 HIS 2 -9
REMARK 465 THR 2 -8
REMARK 465 GLN 2 -7
REMARK 465 PRO 2 -6
REMARK 465 LYS 2 -5
REMARK 465 ALA 2 -4
REMARK 465 THR 2 -3
REMARK 465 SER 2 -2
REMARK 465 THR 2 -1
REMARK 465 GLY 2 0
REMARK 465 GLN 2 227
REMARK 465 VAL 2 228
REMARK 465 ASP 2 229
REMARK 465 ILE 2 230
REMARK 465 THR 2 231
REMARK 465 ALA 2 232
REMARK 465 MET 3 0
REMARK 465 GLN 4 196
REMARK 465 ALA 4 197
REMARK 465 GLN 4 198
REMARK 465 MET 5 -74
REMARK 465 GLN 5 -73
REMARK 465 ALA 5 -72
REMARK 465 ILE 5 -71
REMARK 465 ALA 5 -70
REMARK 465 ASP 5 -69
REMARK 465 SER 5 -68
REMARK 465 PHE 5 -67
REMARK 465 SER 5 -66
REMARK 465 VAL 5 -65
REMARK 465 PRO 5 -64
REMARK 465 ASN 5 -63
REMARK 465 ARG 5 -62
REMARK 465 LEU 5 -61
REMARK 465 VAL 5 -60
REMARK 465 LYS 5 -59
REMARK 465 GLU 5 -58
REMARK 465 LEU 5 -57
REMARK 465 GLN 5 -56
REMARK 465 TYR 5 -55
REMARK 465 ASP 5 -54
REMARK 465 ASN 5 -53
REMARK 465 GLU 5 -52
REMARK 465 GLN 5 -51
REMARK 465 ASN 5 -50
REMARK 465 LEU 5 -49
REMARK 465 GLU 5 -48
REMARK 465 SER 5 -47
REMARK 465 ASP 5 -46
REMARK 465 PHE 5 -45
REMARK 465 VAL 5 -44
REMARK 465 THR 5 -43
REMARK 465 GLY 5 -42
REMARK 465 ALA 5 -41
REMARK 465 SER 5 -40
REMARK 465 GLN 5 -39
REMARK 465 PHE 5 -38
REMARK 465 GLN 5 -37
REMARK 465 ARG 5 -36
REMARK 465 LEU 5 -35
REMARK 465 ALA 5 -34
REMARK 465 PRO 5 -33
REMARK 465 SER 5 -32
REMARK 465 LEU 5 -31
REMARK 465 THR 5 -30
REMARK 465 VAL 5 -29
REMARK 465 PRO 5 -28
REMARK 465 PRO 5 -27
REMARK 465 ILE 5 -26
REMARK 465 ALA 5 -25
REMARK 465 SER 5 -24
REMARK 465 PRO 5 -23
REMARK 465 GLN 5 -22
REMARK 465 GLN 5 -21
REMARK 465 PHE 5 -20
REMARK 465 LEU 5 -19
REMARK 465 ARG 5 -18
REMARK 465 ALA 5 -17
REMARK 465 HIS 5 -16
REMARK 465 THR 5 -15
REMARK 465 ASP 5 -14
REMARK 465 ASP 5 -13
REMARK 465 SER 5 -12
REMARK 465 ARG 5 -11
REMARK 465 ASN 5 -10
REMARK 465 PRO 5 -9
REMARK 465 ASP 5 -8
REMARK 465 CYS 5 -7
REMARK 465 LYS 5 -6
REMARK 465 ILE 5 -5
REMARK 465 LYS 5 -4
REMARK 465 ILE 5 -3
REMARK 465 ALA 5 -2
REMARK 465 HIS 5 -1
REMARK 465 GLY 5 0
REMARK 465 MET 6 -18
REMARK 465 ALA 6 -17
REMARK 465 THR 6 -16
REMARK 465 ILE 6 -15
REMARK 465 ALA 6 -14
REMARK 465 SER 6 -13
REMARK 465 GLU 6 -12
REMARK 465 TYR 6 -11
REMARK 465 SER 6 -10
REMARK 465 SER 6 -9
REMARK 465 GLU 6 -8
REMARK 465 ALA 6 -7
REMARK 465 SER 6 -6
REMARK 465 ASN 6 -5
REMARK 465 THR 6 -4
REMARK 465 PRO 6 -3
REMARK 465 ILE 6 -2
REMARK 465 GLU 6 -1
REMARK 465 HIS 6 0
REMARK 465 MET 7 -32
REMARK 465 ASN 7 -31
REMARK 465 HIS 7 -30
REMARK 465 ASP 7 -29
REMARK 465 PRO 7 -28
REMARK 465 PHE 7 -27
REMARK 465 SER 7 -26
REMARK 465 TRP 7 -25
REMARK 465 GLY 7 -24
REMARK 465 ARG 7 -23
REMARK 465 PRO 7 -22
REMARK 465 ALA 7 -21
REMARK 465 ASP 7 -20
REMARK 465 SER 7 -19
REMARK 465 THR 7 -18
REMARK 465 TYR 7 -17
REMARK 465 GLY 7 -16
REMARK 465 ALA 7 -15
REMARK 465 TYR 7 -14
REMARK 465 ASN 7 -13
REMARK 465 THR 7 -12
REMARK 465 GLN 7 -11
REMARK 465 ILE 7 -10
REMARK 465 ALA 7 -9
REMARK 465 ASN 7 -8
REMARK 465 ALA 7 -7
REMARK 465 GLY 7 -6
REMARK 465 ALA 7 -5
REMARK 465 SER 7 -4
REMARK 465 PRO 7 -3
REMARK 465 MET 7 -2
REMARK 465 VAL 7 -1
REMARK 465 ASN 7 0
REMARK 465 THR 7 230
REMARK 465 GLN 7 231
REMARK 465 LYS 7 232
REMARK 465 ILE 7 233
REMARK 465 MET H 1
REMARK 465 PRO H 2
REMARK 465 PRO H 3
REMARK 465 LYS H 4
REMARK 465 GLU H 5
REMARK 465 ASP H 6
REMARK 465 TRP H 7
REMARK 465 GLU H 8
REMARK 465 LYS H 9
REMARK 465 TYR H 10
REMARK 465 LYS H 11
REMARK 465 ALA H 12
REMARK 465 PRO H 13
REMARK 465 LEU H 14
REMARK 465 GLU H 15
REMARK 465 ASP H 16
REMARK 465 ASP H 17
REMARK 465 ASP H 18
REMARK 465 LYS H 19
REMARK 465 LYS H 20
REMARK 465 PRO H 21
REMARK 465 ASP H 22
REMARK 465 ASP H 23
REMARK 465 ASP H 24
REMARK 465 LYS H 25
REMARK 465 ILE H 26
REMARK 465 VAL H 27
REMARK 465 PRO H 28
REMARK 465 LEU H 29
REMARK 465 THR H 30
REMARK 465 GLU H 31
REMARK 465 GLY H 32
REMARK 465 ASP H 33
REMARK 465 ILE H 34
REMARK 465 GLN H 35
REMARK 465 VAL H 36
REMARK 465 LEU H 37
REMARK 465 LYS H 38
REMARK 465 SER H 39
REMARK 465 TYR H 40
REMARK 465 GLY H 41
REMARK 465 GLY H 108
REMARK 465 ASN H 109
REMARK 465 GLY H 110
REMARK 465 GLU H 111
REMARK 465 SER H 112
REMARK 465 ASP H 113
REMARK 465 GLU H 114
REMARK 465 THR H 115
REMARK 465 THR H 116
REMARK 465 THR H 117
REMARK 465 ASP H 118
REMARK 465 ASN H 119
REMARK 465 ASN H 120
REMARK 465 ASN H 121
REMARK 465 SER H 122
REMARK 465 GLY H 123
REMARK 465 ASN H 124
REMARK 465 SER H 125
REMARK 465 ASN H 126
REMARK 465 SER H 127
REMARK 465 ASN H 128
REMARK 465 SER H 129
REMARK 465 ASN H 130
REMARK 465 GLN H 131
REMARK 465 GLN H 132
REMARK 465 SER H 133
REMARK 465 THR H 134
REMARK 465 ASP H 135
REMARK 465 ALA H 136
REMARK 465 ASP H 137
REMARK 465 GLU H 138
REMARK 465 ASP H 139
REMARK 465 ASP H 140
REMARK 465 GLU H 141
REMARK 465 ASP H 142
REMARK 465 ALA H 143
REMARK 465 MET I 1
REMARK 465 GLY I 2
REMARK 465 GLN I 3
REMARK 465 GLY I 4
REMARK 465 VAL I 5
REMARK 465 SER I 6
REMARK 465 SER I 7
REMARK 465 GLY I 8
REMARK 465 GLN I 9
REMARK 465 ASP I 10
REMARK 465 LYS I 11
REMARK 465 LYS I 12
REMARK 465 LYS I 13
REMARK 465 LYS I 14
REMARK 465 LYS I 15
REMARK 465 GLY I 16
REMARK 465 SER I 17
REMARK 465 ASN I 18
REMARK 465 GLN I 19
REMARK 465 LYS I 20
REMARK 465 PRO I 21
REMARK 465 LYS I 22
REMARK 465 TYR I 23
REMARK 465 GLU I 24
REMARK 465 PRO I 25
REMARK 465 PRO I 26
REMARK 465 VAL I 27
REMARK 465 GLN I 28
REMARK 465 SER I 29
REMARK 465 LYS I 30
REMARK 465 PHE I 31
REMARK 465 GLY I 32
REMARK 465 ARG I 33
REMARK 465 LYS I 34
REMARK 465 LYS I 35
REMARK 465 ARG I 36
REMARK 465 LYS I 37
REMARK 465 GLY I 38
REMARK 465 GLY I 39
REMARK 465 PRO I 40
REMARK 465 ALA I 41
REMARK 465 THR I 42
REMARK 465 ALA I 43
REMARK 465 GLU I 44
REMARK 465 LYS I 45
REMARK 465 LEU I 46
REMARK 465 PRO I 47
REMARK 465 ASN I 48
REMARK 465 ILE I 49
REMARK 465 TYR I 50
REMARK 465 PRO I 51
REMARK 465 SER I 52
REMARK 465 MET K 1
REMARK 465 GLU K 2
REMARK 465 GLU K 3
REMARK 465 LEU K 4
REMARK 465 GLY K 5
REMARK 465 ILE K 6
REMARK 465 VAL K 7
REMARK 465 THR K 8
REMARK 465 PRO K 9
REMARK 465 VAL K 10
REMARK 465 GLU K 11
REMARK 465 LYS K 12
REMARK 465 ALA K 13
REMARK 465 VAL K 14
REMARK 465 GLU K 15
REMARK 465 GLU K 16
REMARK 465 LYS K 17
REMARK 465 PRO K 18
REMARK 465 ALA K 19
REMARK 465 VAL K 20
REMARK 465 LYS K 21
REMARK 465 SER K 22
REMARK 465 TYR K 23
REMARK 465 ALA K 24
REMARK 465 SER K 25
REMARK 465 LEU K 26
REMARK 465 LEU K 27
REMARK 465 ALA K 28
REMARK 465 GLN K 29
REMARK 465 LEU K 30
REMARK 465 ASN K 31
REMARK 465 GLY K 32
REMARK 465 THR K 33
REMARK 465 VAL K 34
REMARK 465 ASN K 35
REMARK 465 ASN K 36
REMARK 465 ASN K 37
REMARK 465 SER K 38
REMARK 465 ALA K 39
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 GLU L 3
REMARK 465 GLU L 4
REMARK 465 GLN L 5
REMARK 465 ASP L 6
REMARK 465 PRO L 7
REMARK 465 LEU L 8
REMARK 465 LEU L 9
REMARK 465 ALA L 10
REMARK 465 GLY L 11
REMARK 465 LEU L 12
REMARK 465 GLY L 13
REMARK 465 GLU L 14
REMARK 465 THR L 15
REMARK 465 SER L 16
REMARK 465 GLY L 17
REMARK 465 ASP L 18
REMARK 465 ASN L 19
REMARK 465 HIS L 20
REMARK 465 THR L 21
REMARK 465 GLN L 22
REMARK 465 GLN L 23
REMARK 465 SER L 24
REMARK 465 HIS L 25
REMARK 465 GLU L 26
REMARK 465 GLN L 27
REMARK 465 GLN L 28
REMARK 465 PRO L 29
REMARK 465 GLU L 30
REMARK 465 GLN L 31
REMARK 465 PRO L 32
REMARK 465 GLN L 33
REMARK 465 GLU L 34
REMARK 465 THR L 35
REMARK 465 GLU L 36
REMARK 465 GLU L 37
REMARK 465 HIS L 38
REMARK 465 HIS L 39
REMARK 465 GLU L 40
REMARK 465 GLU L 41
REMARK 465 GLU L 42
REMARK 465 PRO L 43
REMARK 465 SER L 44
REMARK 465 ARG L 45
REMARK 465 VAL L 46
REMARK 465 ASP L 47
REMARK 465 PRO L 48
REMARK 465 LEU L 437
REMARK 465 MET M 1
REMARK 465 ALA M 2
REMARK 465 THR M 3
REMARK 465 LEU M 4
REMARK 465 GLU M 5
REMARK 465 GLU M 6
REMARK 465 LEU M 7
REMARK 465 ASP M 8
REMARK 465 ALA M 9
REMARK 465 GLN M 10
REMARK 465 THR M 11
REMARK 465 LEU M 12
REMARK 465 PRO M 13
REMARK 465 GLY M 14
REMARK 465 ASP M 15
REMARK 465 ASP M 16
REMARK 465 GLU M 17
REMARK 465 LEU M 18
REMARK 465 ASP M 19
REMARK 465 GLN M 20
REMARK 465 GLU M 21
REMARK 465 ILE M 22
REMARK 465 LEU M 23
REMARK 465 ASN M 24
REMARK 465 LEU M 25
REMARK 465 SER M 26
REMARK 465 MET M 88
REMARK 465 ASN M 89
REMARK 465 GLU M 90
REMARK 465 ILE M 91
REMARK 465 GLU M 92
REMARK 465 ASP M 93
REMARK 465 LYS M 94
REMARK 465 GLU M 95
REMARK 465 ASN M 96
REMARK 465 SER M 97
REMARK 465 GLU M 98
REMARK 465 SER M 99
REMARK 465 THR M 100
REMARK 465 THR M 101
REMARK 465 GLN M 102
REMARK 465 GLY M 103
REMARK 465 GLY M 104
REMARK 465 ASN M 105
REMARK 465 VAL M 106
REMARK 465 ASN M 107
REMARK 465 LEU M 108
REMARK 465 ASP M 109
REMARK 465 ASN M 110
REMARK 465 THR M 111
REMARK 465 ALA M 112
REMARK 465 VAL M 113
REMARK 465 GLY M 114
REMARK 465 MET J 1
REMARK 465 THR J 2
REMARK 465 ALA J 3
REMARK 465 ALA J 4
REMARK 465 VAL J 5
REMARK 465 THR J 6
REMARK 465 SER J 7
REMARK 465 SER J 8
REMARK 465 ASN J 9
REMARK 465 ILE J 10
REMARK 465 VAL J 11
REMARK 465 LEU J 12
REMARK 465 SER J 399
REMARK 465 VAL J 400
REMARK 465 ALA J 401
REMARK 465 LYS J 402
REMARK 465 LEU J 403
REMARK 465 PHE J 404
REMARK 465 LYS J 405
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS J 359 O3' ADP J 501 1.26
REMARK 500 NH1 ARG b 4 OE2 GLU e 117 1.35
REMARK 500 CZ ARG b 4 OE1 GLU e 117 1.43
REMARK 500 NH2 ARG I 340 O3A ATP H 502 1.49
REMARK 500 NH1 ARG b 4 CD GLU e 117 1.55
REMARK 500 NH1 ARG b 4 OE1 GLU e 117 1.61
REMARK 500 CD1 ILE L 183 N6 ATP L 501 1.74
REMARK 500 CZ ARG b 4 CD GLU e 117 1.76
REMARK 500 NE ARG b 4 OE1 GLU e 117 1.97
REMARK 500 NH2 ARG b 4 CD GLU e 117 1.99
REMARK 500 NH1 ARG M 357 O ALA M 380 2.09
REMARK 500 NH2 ARG I 340 PA ATP H 502 2.12
REMARK 500 O TYR 1 193 O LEU 1 196 2.14
REMARK 500 O ALA I 337 NH1 ARG I 343 2.18
REMARK 500 CZ ARG b 4 OE2 GLU e 117 2.18
REMARK 500 NH2 ARG I 340 O5' ATP H 502 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN a 242 C GLN a 242 O -0.229
REMARK 500 PHE b 142 CE1 PHE b 142 CZ 0.123
REMARK 500 PHE b 145 CB PHE b 145 CG -0.111
REMARK 500 ASP b 187 CB ASP b 187 CG 0.172
REMARK 500 LEU b 250 C LEU b 250 O -0.229
REMARK 500 LEU b 250 C LEU b 250 OXT -0.229
REMARK 500 GLU c 15 CB GLU c 15 CG 0.125
REMARK 500 GLU c 15 CG GLU c 15 CD 0.130
REMARK 500 TYR c 145 CD1 TYR c 145 CE1 -0.096
REMARK 500 TYR c 207 CD1 TYR c 207 CE1 -0.133
REMARK 500 TYR c 207 CE2 TYR c 207 CD2 -0.090
REMARK 500 THR c 244 C THR c 244 O -0.229
REMARK 500 SER d 10 CA SER d 10 CB 0.095
REMARK 500 CYS d 30 CB CYS d 30 SG -0.125
REMARK 500 ASN d 176 CB ASN d 176 CG 0.151
REMARK 500 ARG e 12 NE ARG e 12 CZ 0.078
REMARK 500 ARG e 85 NE ARG e 85 CZ 0.082
REMARK 500 ARG e 124 CD ARG e 124 NE 0.107
REMARK 500 GLU e 151 CD GLU e 151 OE1 0.081
REMARK 500 GLU e 242 C GLU e 242 O -0.229
REMARK 500 ARG f 106 CD ARG f 106 NE 0.102
REMARK 500 ILE f 233 C ILE f 233 O -0.229
REMARK 500 ILE f 233 C ILE f 233 OXT -0.230
REMARK 500 PHE g 226 CB PHE g 226 CG -0.129
REMARK 500 ASN g 244 C ASN g 244 O -0.229
REMARK 500 GLY h 47 CA GLY h 47 C -0.103
REMARK 500 THR h 72 C PRO h 73 N -0.118
REMARK 500 GLU h 84 CG GLU h 84 CD 0.090
REMARK 500 ARG h 174 NE ARG h 174 CZ 0.081
REMARK 500 LEU h 196 C LEU h 196 O -0.229
REMARK 500 LEU h 196 C LEU h 196 OXT -0.229
REMARK 500 GLU i 150 CB GLU i 150 CG -0.116
REMARK 500 TYR i 190 CD1 TYR i 190 CE1 -0.135
REMARK 500 TYR i 190 CE2 TYR i 190 CD2 -0.133
REMARK 500 PHE i 205 CB PHE i 205 CG -0.131
REMARK 500 GLU i 226 C GLU i 226 O -0.229
REMARK 500 SER j 36 CA SER j 36 CB -0.092
REMARK 500 GLU j 84 CG GLU j 84 CD 0.143
REMARK 500 ARG j 97 CZ ARG j 97 NH2 0.082
REMARK 500 GLY j 127 CA GLY j 127 C -0.106
REMARK 500 TRP j 182 CB TRP j 182 CG -0.141
REMARK 500 GLU k 49 CG GLU k 49 CD 0.144
REMARK 500 GLU k 58 CB GLU k 58 CG 0.167
REMARK 500 GLU k 58 CG GLU k 58 CD 0.098
REMARK 500 TYR k 148 CD1 TYR k 148 CE1 -0.107
REMARK 500 TYR k 148 CE2 TYR k 148 CD2 -0.111
REMARK 500 PHE k 195 C PHE k 195 O -0.229
REMARK 500 ARG l 159 CZ ARG l 159 NH2 0.090
REMARK 500 ASP l 168 CB ASP l 168 CG 0.135
REMARK 500 GLU l 202 CG GLU l 202 CD -0.096
REMARK 500
REMARK 500 THIS ENTRY HAS 133 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG a 5 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG a 5 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG a 15 CG - CD - NE ANGL. DEV. = 12.7 DEGREES
REMARK 500 VAL a 19 CA - CB - CG2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 TYR a 21 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 TYR a 62 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG a 122 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG a 122 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 SER a 136 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 TYR a 146 CB - CG - CD2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 TYR a 146 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TYR a 153 CG - CD2 - CE2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TYR a 154 CG - CD2 - CE2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG b 4 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR b 5 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 PHE b 12 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP b 22 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP b 22 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 TYR b 23 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR b 23 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG b 99 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 TYR b 148 CG - CD1 - CE1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ALA b 170 N - CA - CB ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG b 178 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP b 220 CB - CG - OD1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASP b 220 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG b 234 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 GLU c 15 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG c 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TYR c 97 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG c 112 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG c 128 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG c 128 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR c 148 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP d 3 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 TYR d 20 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR d 20 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG d 47 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG d 88 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TYR d 106 CD1 - CE1 - CZ ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG d 117 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG d 117 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 TYR d 146 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 SER d 223 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG e 12 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TYR e 18 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR e 18 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG e 45 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG e 85 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TYR e 94 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 302 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU a 16 109.09 -59.43
REMARK 500 ASN a 27 76.73 -102.54
REMARK 500 TYR a 62 9.33 -155.68
REMARK 500 ASP a 106 -50.26 -28.64
REMARK 500 ASP a 138 177.41 -59.76
REMARK 500 LYS a 165 36.31 -83.64
REMARK 500 SER a 210 -146.53 -104.91
REMARK 500 LYS a 221 108.71 -59.69
REMARK 500 ASP a 222 13.78 82.15
REMARK 500 THR b 2 60.64 65.61
REMARK 500 ALA b 39 -152.63 -122.74
REMARK 500 LEU b 67 -68.71 -92.74
REMARK 500 PRO b 69 -23.54 -39.69
REMARK 500 TYR b 97 -64.76 -153.60
REMARK 500 TYR b 101 2.22 -162.70
REMARK 500 GLU b 103 161.63 -49.99
REMARK 500 GLU b 184 156.47 -48.94
REMARK 500 TYR b 224 78.80 -168.97
REMARK 500 ARG b 236 114.44 -160.68
REMARK 500 ALA b 249 33.67 -93.23
REMARK 500 SER c 2 20.90 -150.31
REMARK 500 ARG c 8 78.77 20.20
REMARK 500 ASP c 41 22.53 -143.34
REMARK 500 VAL c 51 73.34 49.17
REMARK 500 GLU c 63 -0.12 -164.83
REMARK 500 LYS c 64 -23.69 -156.75
REMARK 500 ALA c 81 -70.41 -52.56
REMARK 500 ASP c 140 -156.46 -108.11
REMARK 500 TYR c 143 -11.70 -159.17
REMARK 500 ASN c 155 135.08 -35.90
REMARK 500 MET c 183 132.70 -30.70
REMARK 500 ALA c 192 -73.61 -58.83
REMARK 500 SER c 202 169.31 -44.69
REMARK 500 ALA c 219 94.31 79.22
REMARK 500 ASN c 220 70.11 76.83
REMARK 500 ASP c 221 -149.07 51.96
REMARK 500 ASP d 3 6.27 -161.00
REMARK 500 ASN d 38 18.33 -173.64
REMARK 500 HIS d 68 19.86 -159.55
REMARK 500 ARG d 139 18.88 58.91
REMARK 500 ASP d 140 -161.55 -126.69
REMARK 500 ASP d 141 -22.95 -144.96
REMARK 500 GLU d 181 88.59 -170.26
REMARK 500 GLN d 202 73.83 44.48
REMARK 500 THR d 203 122.79 42.88
REMARK 500 ASP d 216 79.55 46.05
REMARK 500 SER e 5 7.79 -161.09
REMARK 500 THR e 34 -155.16 -108.73
REMARK 500 ARG e 45 86.65 40.26
REMARK 500 LYS e 58 3.25 -155.28
REMARK 500
REMARK 500 THIS ENTRY HAS 441 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR a 148 ASP a 149 -147.79
REMARK 500 LEU b 134 LEU b 135 147.80
REMARK 500 ILE b 213 ILE b 214 145.15
REMARK 500 PHE c 134 ILE c 135 141.98
REMARK 500 ASP n 77 ASN n 78 -144.22
REMARK 500 LEU B 134 LEU B 135 146.59
REMARK 500 SER C 61 THR C 62 144.93
REMARK 500 ARG E 128 PRO E 129 -119.17
REMARK 500 SER 2 171 ASN 2 172 -147.19
REMARK 500 THR 7 9 SER 7 10 146.67
REMARK 500 ARG H 367 PRO H 368 -129.88
REMARK 500 SER I 182 ASP I 183 140.47
REMARK 500 GLY I 186 LEU I 187 -147.41
REMARK 500 ILE I 339 ARG I 340 124.10
REMARK 500 GLY I 342 ARG I 343 138.73
REMARK 500 VAL L 131 ARG L 132 149.75
REMARK 500 SER L 292 GLU L 293 149.24
REMARK 500 LEU L 338 ARG L 339 -138.26
REMARK 500 ARG L 342 LEU L 343 -135.80
REMARK 500 PHE L 376 GLU L 377 -140.76
REMARK 500 PHE M 291 ASP M 292 147.77
REMARK 500 THR J 378 GLN J 379 -147.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR a 146 0.09 SIDE CHAIN
REMARK 500 TYR b 23 0.10 SIDE CHAIN
REMARK 500 ARG b 83 0.11 SIDE CHAIN
REMARK 500 ARG c 4 0.09 SIDE CHAIN
REMARK 500 PHE c 134 0.08 SIDE CHAIN
REMARK 500 TYR f 23 0.07 SIDE CHAIN
REMARK 500 TYR f 86 0.08 SIDE CHAIN
REMARK 500 TYR f 93 0.09 SIDE CHAIN
REMARK 500 TYR f 127 0.07 SIDE CHAIN
REMARK 500 ARG f 163 0.08 SIDE CHAIN
REMARK 500 TYR f 224 0.11 SIDE CHAIN
REMARK 500 TYR f 232 0.09 SIDE CHAIN
REMARK 500 ARG g 16 0.12 SIDE CHAIN
REMARK 500 TYR i 124 0.11 SIDE CHAIN
REMARK 500 TYR j 68 0.08 SIDE CHAIN
REMARK 500 TYR k 59 0.07 SIDE CHAIN
REMARK 500 ARG l 7 0.07 SIDE CHAIN
REMARK 500 TYR l 104 0.08 SIDE CHAIN
REMARK 500 TYR m 98 0.07 SIDE CHAIN
REMARK 500 TYR n 101 0.08 SIDE CHAIN
REMARK 500 ARG A 68 0.08 SIDE CHAIN
REMARK 500 ARG A 82 0.09 SIDE CHAIN
REMARK 500 ARG A 96 0.12 SIDE CHAIN
REMARK 500 TYR A 97 0.07 SIDE CHAIN
REMARK 500 TYR A 119 0.09 SIDE CHAIN
REMARK 500 TYR A 146 0.08 SIDE CHAIN
REMARK 500 TYR A 153 0.12 SIDE CHAIN
REMARK 500 ARG B 4 0.16 SIDE CHAIN
REMARK 500 TYR B 5 0.08 SIDE CHAIN
REMARK 500 TYR B 156 0.09 SIDE CHAIN
REMARK 500 TYR B 224 0.11 SIDE CHAIN
REMARK 500 ARG C 8 0.11 SIDE CHAIN
REMARK 500 ARG C 17 0.08 SIDE CHAIN
REMARK 500 TYR C 121 0.08 SIDE CHAIN
REMARK 500 TYR D 2 0.13 SIDE CHAIN
REMARK 500 TYR D 110 0.10 SIDE CHAIN
REMARK 500 ARG E 2 0.10 SIDE CHAIN
REMARK 500 PHE E 130 0.08 SIDE CHAIN
REMARK 500 TYR E 157 0.10 SIDE CHAIN
REMARK 500 TYR F 5 0.11 SIDE CHAIN
REMARK 500 ARG F 17 0.07 SIDE CHAIN
REMARK 500 TYR F 23 0.07 SIDE CHAIN
REMARK 500 ARG F 81 0.10 SIDE CHAIN
REMARK 500 TYR F 86 0.10 SIDE CHAIN
REMARK 500 TYR F 93 0.07 SIDE CHAIN
REMARK 500 TYR F 136 0.11 SIDE CHAIN
REMARK 500 TYR F 156 0.11 SIDE CHAIN
REMARK 500 ARG G 82 0.11 SIDE CHAIN
REMARK 500 ARG G 126 0.10 SIDE CHAIN
REMARK 500 TYR 1 70 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 65 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG E 128 -11.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR H 257 OG1
REMARK 620 2 ATP H 502 O2B 86.2
REMARK 620 3 ATP H 502 O2G 148.9 65.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 230 OG1
REMARK 620 2 ATP I 501 O2B 55.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR K 220 OG1
REMARK 620 2 ATP K 501 O1G 153.1
REMARK 620 3 ATP K 501 O1B 87.1 67.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR L 229 OG1
REMARK 620 2 ATP L 501 O2G 117.4
REMARK 620 3 ATP L 501 O2B 56.5 61.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG M 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR M 229 OG1
REMARK 620 2 ATP M 501 O2G 153.2
REMARK 620 3 ATP M 501 O1B 97.1 58.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR J 196 OG1
REMARK 620 2 ADP J 501 O3B 103.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP H 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP I 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP K 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP L 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP M 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG M 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP J 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-3535 RELATED DB: EMDB
REMARK 900 26S PROTEASOME IN PRESENCE OF ATP (S2)
DBREF 5MPA a -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5MPA b 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5MPA c 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5MPA d -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5MPA e -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5MPA f 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5MPA g -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5MPA h -18 196 UNP P38624 PSB1_YEAST 1 215
DBREF 5MPA i -28 232 UNP P25043 PSB2_YEAST 1 261
DBREF 5MPA j 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5MPA k 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5MPA l -74 212 UNP P30656 PSB5_YEAST 1 287
DBREF 5MPA m -18 222 UNP P23724 PSB6_YEAST 1 241
DBREF 5MPA n -32 233 UNP P30657 PSB7_YEAST 1 266
DBREF 5MPA A -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5MPA B 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5MPA C 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5MPA D -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5MPA E -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5MPA F 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5MPA G -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5MPA 1 -18 196 UNP P38624 PSB1_YEAST 1 215
DBREF 5MPA 2 -28 232 UNP P25043 PSB2_YEAST 1 261
DBREF 5MPA 3 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5MPA 4 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5MPA 5 -74 212 UNP P30656 PSB5_YEAST 1 287
DBREF 5MPA 6 -18 222 UNP P23724 PSB6_YEAST 1 241
DBREF 5MPA 7 -32 233 UNP P30657 PSB7_YEAST 1 266
DBREF 5MPA H 1 467 UNP P33299 PRS7_YEAST 1 467
DBREF 5MPA I 1 437 UNP P40327 PRS4_YEAST 1 437
DBREF 5MPA K 1 428 UNP P33298 PRS6B_YEAST 1 428
DBREF 5MPA L 1 437 UNP P53549 PRS10_YEAST 1 437
DBREF 5MPA M 1 434 UNP P33297 PRS6A_YEAST 1 434
DBREF 5MPA J 1 405 UNP Q01939 PRS8_YEAST 1 405
SEQRES 1 a 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 a 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 a 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 a 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 a 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 a 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 a 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 a 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 a 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 a 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 a 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 a 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 a 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 a 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 a 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 a 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 a 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 a 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 a 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 a 252 ILE ALA GLU GLN ASP
SEQRES 1 b 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 b 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 b 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 b 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 b 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 b 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 b 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 b 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 b 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 b 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 b 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 b 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 b 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 b 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 b 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 b 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 b 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 b 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 b 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 b 250 GLU ALA LEU
SEQRES 1 c 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 c 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 c 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 c 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 c 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 c 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 c 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 c 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 c 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 c 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 c 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 c 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 c 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 c 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 c 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 c 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 c 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 c 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 c 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 c 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 d 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 d 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 d 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 d 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 d 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 d 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 d 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 d 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 d 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 d 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 d 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 d 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 d 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 d 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 d 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 d 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 d 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 d 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 d 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 d 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 e 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 e 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 e 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 e 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 e 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 e 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 e 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 e 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 e 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 e 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 e 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 e 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 e 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 e 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 e 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 e 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 e 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 e 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 e 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 e 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 f 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 f 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 f 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 f 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 f 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 f 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 f 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 f 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 f 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 f 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 f 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 f 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 f 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 f 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 f 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 f 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 f 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 f 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 g 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 g 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 g 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 g 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 g 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 g 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 g 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 g 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 g 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 g 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 g 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 g 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 g 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 g 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 g 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 g 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 g 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 g 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 g 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 g 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 g 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 g 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 g 288 LEU GLU
SEQRES 1 h 215 MET ASN GLY ILE GLN VAL ASP ILE ASN ARG LEU LYS LYS
SEQRES 2 h 215 GLY GLU VAL SER LEU GLY THR SER ILE MET ALA VAL THR
SEQRES 3 h 215 PHE LYS ASP GLY VAL ILE LEU GLY ALA ASP SER ARG THR
SEQRES 4 h 215 THR THR GLY ALA TYR ILE ALA ASN ARG VAL THR ASP LYS
SEQRES 5 h 215 LEU THR ARG VAL HIS ASP LYS ILE TRP CYS CYS ARG SER
SEQRES 6 h 215 GLY SER ALA ALA ASP THR GLN ALA ILE ALA ASP ILE VAL
SEQRES 7 h 215 GLN TYR HIS LEU GLU LEU TYR THR SER GLN TYR GLY THR
SEQRES 8 h 215 PRO SER THR GLU THR ALA ALA SER VAL PHE LYS GLU LEU
SEQRES 9 h 215 CYS TYR GLU ASN LYS ASP ASN LEU THR ALA GLY ILE ILE
SEQRES 10 h 215 VAL ALA GLY TYR ASP ASP LYS ASN LYS GLY GLU VAL TYR
SEQRES 11 h 215 THR ILE PRO LEU GLY GLY SER VAL HIS LYS LEU PRO TYR
SEQRES 12 h 215 ALA ILE ALA GLY SER GLY SER THR PHE ILE TYR GLY TYR
SEQRES 13 h 215 CYS ASP LYS ASN PHE ARG GLU ASN MET SER LYS GLU GLU
SEQRES 14 h 215 THR VAL ASP PHE ILE LYS HIS SER LEU SER GLN ALA ILE
SEQRES 15 h 215 LYS TRP ASP GLY SER SER GLY GLY VAL ILE ARG MET VAL
SEQRES 16 h 215 VAL LEU THR ALA ALA GLY VAL GLU ARG LEU ILE PHE TYR
SEQRES 17 h 215 PRO ASP GLU TYR GLU GLN LEU
SEQRES 1 i 261 MET ALA GLY LEU SER PHE ASP ASN TYR GLN ARG ASN ASN
SEQRES 2 i 261 PHE LEU ALA GLU ASN SER HIS THR GLN PRO LYS ALA THR
SEQRES 3 i 261 SER THR GLY THR THR ILE VAL GLY VAL LYS PHE ASN ASN
SEQRES 4 i 261 GLY VAL VAL ILE ALA ALA ASP THR ARG SER THR GLN GLY
SEQRES 5 i 261 PRO ILE VAL ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG
SEQRES 6 i 261 ILE SER PRO LYS ILE TRP CYS ALA GLY ALA GLY THR ALA
SEQRES 7 i 261 ALA ASP THR GLU ALA VAL THR GLN LEU ILE GLY SER ASN
SEQRES 8 i 261 ILE GLU LEU HIS SER LEU TYR THR SER ARG GLU PRO ARG
SEQRES 9 i 261 VAL VAL SER ALA LEU GLN MET LEU LYS GLN HIS LEU PHE
SEQRES 10 i 261 LYS TYR GLN GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA
SEQRES 11 i 261 GLY VAL ASP PRO THR GLY SER HIS LEU PHE SER ILE HIS
SEQRES 12 i 261 ALA HIS GLY SER THR ASP VAL GLY TYR TYR LEU SER LEU
SEQRES 13 i 261 GLY SER GLY SER LEU ALA ALA MET ALA VAL LEU GLU SER
SEQRES 14 i 261 HIS TRP LYS GLN ASP LEU THR LYS GLU GLU ALA ILE LYS
SEQRES 15 i 261 LEU ALA SER ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP
SEQRES 16 i 261 LEU GLY SER GLY SER ASN VAL ASP VAL CYS VAL MET GLU
SEQRES 17 i 261 ILE GLY LYS ASP ALA GLU TYR LEU ARG ASN TYR LEU THR
SEQRES 18 i 261 PRO ASN VAL ARG GLU GLU LYS GLN LYS SER TYR LYS PHE
SEQRES 19 i 261 PRO ARG GLY THR THR ALA VAL LEU LYS GLU SER ILE VAL
SEQRES 20 i 261 ASN ILE CYS ASP ILE GLN GLU GLU GLN VAL ASP ILE THR
SEQRES 21 i 261 ALA
SEQRES 1 j 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 j 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 j 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 j 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 j 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 j 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 j 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 j 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 j 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 j 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 j 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 j 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 j 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 j 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 j 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 j 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 k 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 k 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 k 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 k 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 k 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 k 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 k 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 k 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 k 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 k 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 k 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 k 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 k 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 k 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 k 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 k 198 GLN ALA GLN
SEQRES 1 l 287 MET GLN ALA ILE ALA ASP SER PHE SER VAL PRO ASN ARG
SEQRES 2 l 287 LEU VAL LYS GLU LEU GLN TYR ASP ASN GLU GLN ASN LEU
SEQRES 3 l 287 GLU SER ASP PHE VAL THR GLY ALA SER GLN PHE GLN ARG
SEQRES 4 l 287 LEU ALA PRO SER LEU THR VAL PRO PRO ILE ALA SER PRO
SEQRES 5 l 287 GLN GLN PHE LEU ARG ALA HIS THR ASP ASP SER ARG ASN
SEQRES 6 l 287 PRO ASP CYS LYS ILE LYS ILE ALA HIS GLY THR THR THR
SEQRES 7 l 287 LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE VAL ALA VAL
SEQRES 8 l 287 ASP SER ARG ALA THR ALA GLY ASN TRP VAL ALA SER GLN
SEQRES 9 l 287 THR VAL LYS LYS VAL ILE GLU ILE ASN PRO PHE LEU LEU
SEQRES 10 l 287 GLY THR MET ALA GLY GLY ALA ALA ASP CYS GLN PHE TRP
SEQRES 11 l 287 GLU THR TRP LEU GLY SER GLN CYS ARG LEU HIS GLU LEU
SEQRES 12 l 287 ARG GLU LYS GLU ARG ILE SER VAL ALA ALA ALA SER LYS
SEQRES 13 l 287 ILE LEU SER ASN LEU VAL TYR GLN TYR LYS GLY ALA GLY
SEQRES 14 l 287 LEU SER MET GLY THR MET ILE CYS GLY TYR THR ARG LYS
SEQRES 15 l 287 GLU GLY PRO THR ILE TYR TYR VAL ASP SER ASP GLY THR
SEQRES 16 l 287 ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY SER GLY GLN
SEQRES 17 l 287 THR PHE ALA TYR GLY VAL LEU ASP SER ASN TYR LYS TRP
SEQRES 18 l 287 ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY LYS ARG
SEQRES 19 l 287 SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR SER GLY
SEQRES 20 l 287 GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP GLY TRP
SEQRES 21 l 287 ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU PHE TRP
SEQRES 22 l 287 LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN VAL ILE
SEQRES 23 l 287 GLY
SEQRES 1 m 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 m 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 m 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 m 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 m 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 m 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 m 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 m 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 m 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 m 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 m 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 m 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 m 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 m 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 m 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 m 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 m 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 m 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 m 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 n 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 n 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 n 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 n 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 n 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 n 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 n 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 n 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 n 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 n 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 n 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 n 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 n 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 n 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 n 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 n 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 n 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 n 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 n 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 n 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 n 266 TYR GLY THR GLN LYS ILE
SEQRES 1 A 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 A 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 A 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 A 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 A 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 A 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 A 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 A 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 A 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 A 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 A 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 A 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 A 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 A 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 A 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 A 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 A 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 A 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 A 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 A 252 ILE ALA GLU GLN ASP
SEQRES 1 B 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 B 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 B 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 B 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 B 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 B 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 B 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 B 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 B 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 B 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 B 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 B 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 B 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 B 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 B 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 B 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 B 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 B 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 B 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 B 250 GLU ALA LEU
SEQRES 1 C 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 C 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 C 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 C 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 C 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 C 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 C 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 C 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 C 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 C 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 C 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 C 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 C 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 C 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 C 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 C 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 C 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 C 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 C 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 C 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 D 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 D 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 D 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 D 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 D 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 D 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 D 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 D 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 D 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 D 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 D 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 D 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 D 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 D 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 D 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 D 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 D 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 D 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 D 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 D 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 E 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 E 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 E 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 E 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 E 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 E 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 E 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 E 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 E 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 E 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 E 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 E 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 E 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 E 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 E 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 E 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 E 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 E 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 E 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 E 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 F 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 F 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 F 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 F 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 F 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 F 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 F 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 F 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 F 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 F 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 F 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 F 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 F 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 F 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 F 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 F 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 F 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 F 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 G 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 G 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 G 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 G 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 G 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 G 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 G 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 G 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 G 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 G 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 G 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 G 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 G 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 G 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 G 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 G 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 G 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 G 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 G 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 G 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 G 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 G 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 G 288 LEU GLU
SEQRES 1 1 215 MET ASN GLY ILE GLN VAL ASP ILE ASN ARG LEU LYS LYS
SEQRES 2 1 215 GLY GLU VAL SER LEU GLY THR SER ILE MET ALA VAL THR
SEQRES 3 1 215 PHE LYS ASP GLY VAL ILE LEU GLY ALA ASP SER ARG THR
SEQRES 4 1 215 THR THR GLY ALA TYR ILE ALA ASN ARG VAL THR ASP LYS
SEQRES 5 1 215 LEU THR ARG VAL HIS ASP LYS ILE TRP CYS CYS ARG SER
SEQRES 6 1 215 GLY SER ALA ALA ASP THR GLN ALA ILE ALA ASP ILE VAL
SEQRES 7 1 215 GLN TYR HIS LEU GLU LEU TYR THR SER GLN TYR GLY THR
SEQRES 8 1 215 PRO SER THR GLU THR ALA ALA SER VAL PHE LYS GLU LEU
SEQRES 9 1 215 CYS TYR GLU ASN LYS ASP ASN LEU THR ALA GLY ILE ILE
SEQRES 10 1 215 VAL ALA GLY TYR ASP ASP LYS ASN LYS GLY GLU VAL TYR
SEQRES 11 1 215 THR ILE PRO LEU GLY GLY SER VAL HIS LYS LEU PRO TYR
SEQRES 12 1 215 ALA ILE ALA GLY SER GLY SER THR PHE ILE TYR GLY TYR
SEQRES 13 1 215 CYS ASP LYS ASN PHE ARG GLU ASN MET SER LYS GLU GLU
SEQRES 14 1 215 THR VAL ASP PHE ILE LYS HIS SER LEU SER GLN ALA ILE
SEQRES 15 1 215 LYS TRP ASP GLY SER SER GLY GLY VAL ILE ARG MET VAL
SEQRES 16 1 215 VAL LEU THR ALA ALA GLY VAL GLU ARG LEU ILE PHE TYR
SEQRES 17 1 215 PRO ASP GLU TYR GLU GLN LEU
SEQRES 1 2 261 MET ALA GLY LEU SER PHE ASP ASN TYR GLN ARG ASN ASN
SEQRES 2 2 261 PHE LEU ALA GLU ASN SER HIS THR GLN PRO LYS ALA THR
SEQRES 3 2 261 SER THR GLY THR THR ILE VAL GLY VAL LYS PHE ASN ASN
SEQRES 4 2 261 GLY VAL VAL ILE ALA ALA ASP THR ARG SER THR GLN GLY
SEQRES 5 2 261 PRO ILE VAL ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG
SEQRES 6 2 261 ILE SER PRO LYS ILE TRP CYS ALA GLY ALA GLY THR ALA
SEQRES 7 2 261 ALA ASP THR GLU ALA VAL THR GLN LEU ILE GLY SER ASN
SEQRES 8 2 261 ILE GLU LEU HIS SER LEU TYR THR SER ARG GLU PRO ARG
SEQRES 9 2 261 VAL VAL SER ALA LEU GLN MET LEU LYS GLN HIS LEU PHE
SEQRES 10 2 261 LYS TYR GLN GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA
SEQRES 11 2 261 GLY VAL ASP PRO THR GLY SER HIS LEU PHE SER ILE HIS
SEQRES 12 2 261 ALA HIS GLY SER THR ASP VAL GLY TYR TYR LEU SER LEU
SEQRES 13 2 261 GLY SER GLY SER LEU ALA ALA MET ALA VAL LEU GLU SER
SEQRES 14 2 261 HIS TRP LYS GLN ASP LEU THR LYS GLU GLU ALA ILE LYS
SEQRES 15 2 261 LEU ALA SER ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP
SEQRES 16 2 261 LEU GLY SER GLY SER ASN VAL ASP VAL CYS VAL MET GLU
SEQRES 17 2 261 ILE GLY LYS ASP ALA GLU TYR LEU ARG ASN TYR LEU THR
SEQRES 18 2 261 PRO ASN VAL ARG GLU GLU LYS GLN LYS SER TYR LYS PHE
SEQRES 19 2 261 PRO ARG GLY THR THR ALA VAL LEU LYS GLU SER ILE VAL
SEQRES 20 2 261 ASN ILE CYS ASP ILE GLN GLU GLU GLN VAL ASP ILE THR
SEQRES 21 2 261 ALA
SEQRES 1 3 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 3 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 3 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 3 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 3 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 3 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 3 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 3 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 3 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 3 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 3 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 3 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 3 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 3 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 3 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 3 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 4 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 4 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 4 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 4 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 4 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 4 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 4 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 4 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 4 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 4 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 4 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 4 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 4 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 4 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 4 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 4 198 GLN ALA GLN
SEQRES 1 5 287 MET GLN ALA ILE ALA ASP SER PHE SER VAL PRO ASN ARG
SEQRES 2 5 287 LEU VAL LYS GLU LEU GLN TYR ASP ASN GLU GLN ASN LEU
SEQRES 3 5 287 GLU SER ASP PHE VAL THR GLY ALA SER GLN PHE GLN ARG
SEQRES 4 5 287 LEU ALA PRO SER LEU THR VAL PRO PRO ILE ALA SER PRO
SEQRES 5 5 287 GLN GLN PHE LEU ARG ALA HIS THR ASP ASP SER ARG ASN
SEQRES 6 5 287 PRO ASP CYS LYS ILE LYS ILE ALA HIS GLY THR THR THR
SEQRES 7 5 287 LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE VAL ALA VAL
SEQRES 8 5 287 ASP SER ARG ALA THR ALA GLY ASN TRP VAL ALA SER GLN
SEQRES 9 5 287 THR VAL LYS LYS VAL ILE GLU ILE ASN PRO PHE LEU LEU
SEQRES 10 5 287 GLY THR MET ALA GLY GLY ALA ALA ASP CYS GLN PHE TRP
SEQRES 11 5 287 GLU THR TRP LEU GLY SER GLN CYS ARG LEU HIS GLU LEU
SEQRES 12 5 287 ARG GLU LYS GLU ARG ILE SER VAL ALA ALA ALA SER LYS
SEQRES 13 5 287 ILE LEU SER ASN LEU VAL TYR GLN TYR LYS GLY ALA GLY
SEQRES 14 5 287 LEU SER MET GLY THR MET ILE CYS GLY TYR THR ARG LYS
SEQRES 15 5 287 GLU GLY PRO THR ILE TYR TYR VAL ASP SER ASP GLY THR
SEQRES 16 5 287 ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY SER GLY GLN
SEQRES 17 5 287 THR PHE ALA TYR GLY VAL LEU ASP SER ASN TYR LYS TRP
SEQRES 18 5 287 ASP LEU SER VAL GLU ASP ALA LEU TYR LEU GLY LYS ARG
SEQRES 19 5 287 SER ILE LEU ALA ALA ALA HIS ARG ASP ALA TYR SER GLY
SEQRES 20 5 287 GLY SER VAL ASN LEU TYR HIS VAL THR GLU ASP GLY TRP
SEQRES 21 5 287 ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU LEU PHE TRP
SEQRES 22 5 287 LYS VAL LYS GLU GLU GLU GLY SER PHE ASN ASN VAL ILE
SEQRES 23 5 287 GLY
SEQRES 1 6 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 6 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 6 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 6 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 6 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 6 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 6 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 6 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 6 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 6 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 6 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 6 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 6 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 6 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 6 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 6 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 6 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 6 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 6 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 7 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 7 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 7 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 7 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 7 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 7 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 7 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 7 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 7 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 7 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 7 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 7 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 7 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 7 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 7 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 7 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 7 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 7 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 7 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 7 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 7 266 TYR GLY THR GLN LYS ILE
SEQRES 1 H 467 MET PRO PRO LYS GLU ASP TRP GLU LYS TYR LYS ALA PRO
SEQRES 2 H 467 LEU GLU ASP ASP ASP LYS LYS PRO ASP ASP ASP LYS ILE
SEQRES 3 H 467 VAL PRO LEU THR GLU GLY ASP ILE GLN VAL LEU LYS SER
SEQRES 4 H 467 TYR GLY ALA ALA PRO TYR ALA ALA LYS LEU LYS GLN THR
SEQRES 5 H 467 GLU ASN ASP LEU LYS ASP ILE GLU ALA ARG ILE LYS GLU
SEQRES 6 H 467 LYS ALA GLY VAL LYS GLU SER ASP THR GLY LEU ALA PRO
SEQRES 7 H 467 SER HIS LEU TRP ASP ILE MET GLY ASP ARG GLN ARG LEU
SEQRES 8 H 467 GLY GLU GLU HIS PRO LEU GLN VAL ALA ARG CYS THR LYS
SEQRES 9 H 467 ILE ILE LYS GLY ASN GLY GLU SER ASP GLU THR THR THR
SEQRES 10 H 467 ASP ASN ASN ASN SER GLY ASN SER ASN SER ASN SER ASN
SEQRES 11 H 467 GLN GLN SER THR ASP ALA ASP GLU ASP ASP GLU ASP ALA
SEQRES 12 H 467 LYS TYR VAL ILE ASN LEU LYS GLN ILE ALA LYS PHE VAL
SEQRES 13 H 467 VAL GLY LEU GLY GLU ARG VAL SER PRO THR ASP ILE GLU
SEQRES 14 H 467 GLU GLY MET ARG VAL GLY VAL ASP ARG SER LYS TYR ASN
SEQRES 15 H 467 ILE GLU LEU PRO LEU PRO PRO ARG ILE ASP PRO SER VAL
SEQRES 16 H 467 THR MET MET THR VAL GLU GLU LYS PRO ASP VAL THR TYR
SEQRES 17 H 467 SER ASP VAL GLY GLY CYS LYS ASP GLN ILE GLU LYS LEU
SEQRES 18 H 467 ARG GLU VAL VAL GLU LEU PRO LEU LEU SER PRO GLU ARG
SEQRES 19 H 467 PHE ALA THR LEU GLY ILE ASP PRO PRO LYS GLY ILE LEU
SEQRES 20 H 467 LEU TYR GLY PRO PRO GLY THR GLY LYS THR LEU CYS ALA
SEQRES 21 H 467 ARG ALA VAL ALA ASN ARG THR ASP ALA THR PHE ILE ARG
SEQRES 22 H 467 VAL ILE GLY SER GLU LEU VAL GLN LYS TYR VAL GLY GLU
SEQRES 23 H 467 GLY ALA ARG MET VAL ARG GLU LEU PHE GLU MET ALA ARG
SEQRES 24 H 467 THR LYS LYS ALA CYS ILE ILE PHE PHE ASP GLU ILE ASP
SEQRES 25 H 467 ALA VAL GLY GLY ALA ARG PHE ASP ASP GLY ALA GLY GLY
SEQRES 26 H 467 ASP ASN GLU VAL GLN ARG THR MET LEU GLU LEU ILE THR
SEQRES 27 H 467 GLN LEU ASP GLY PHE ASP PRO ARG GLY ASN ILE LYS VAL
SEQRES 28 H 467 MET PHE ALA THR ASN ARG PRO ASN THR LEU ASP PRO ALA
SEQRES 29 H 467 LEU LEU ARG PRO GLY ARG ILE ASP ARG LYS VAL GLU PHE
SEQRES 30 H 467 SER LEU PRO ASP LEU GLU GLY ARG ALA ASN ILE PHE ARG
SEQRES 31 H 467 ILE HIS SER LYS SER MET SER VAL GLU ARG GLY ILE ARG
SEQRES 32 H 467 TRP GLU LEU ILE SER ARG LEU CYS PRO ASN SER THR GLY
SEQRES 33 H 467 ALA GLU LEU ARG SER VAL CYS THR GLU ALA GLY MET PHE
SEQRES 34 H 467 ALA ILE ARG ALA ARG ARG LYS VAL ALA THR GLU LYS ASP
SEQRES 35 H 467 PHE LEU LYS ALA VAL ASP LYS VAL ILE SER GLY TYR LYS
SEQRES 36 H 467 LYS PHE SER SER THR SER ARG TYR MET GLN TYR ASN
SEQRES 1 I 437 MET GLY GLN GLY VAL SER SER GLY GLN ASP LYS LYS LYS
SEQRES 2 I 437 LYS LYS GLY SER ASN GLN LYS PRO LYS TYR GLU PRO PRO
SEQRES 3 I 437 VAL GLN SER LYS PHE GLY ARG LYS LYS ARG LYS GLY GLY
SEQRES 4 I 437 PRO ALA THR ALA GLU LYS LEU PRO ASN ILE TYR PRO SER
SEQRES 5 I 437 THR ARG CYS LYS LEU LYS LEU LEU ARG MET GLU ARG ILE
SEQRES 6 I 437 LYS ASP HIS LEU LEU LEU GLU GLU GLU PHE VAL SER ASN
SEQRES 7 I 437 SER GLU ILE LEU LYS PRO PHE GLU LYS LYS GLN GLU GLU
SEQRES 8 I 437 GLU LYS LYS GLN LEU GLU GLU ILE ARG GLY ASN PRO LEU
SEQRES 9 I 437 SER ILE GLY THR LEU GLU GLU ILE ILE ASP ASP ASP HIS
SEQRES 10 I 437 ALA ILE VAL THR SER PRO THR MET PRO ASP TYR TYR VAL
SEQRES 11 I 437 SER ILE LEU SER PHE VAL ASP LYS GLU LEU LEU GLU PRO
SEQRES 12 I 437 GLY CYS SER VAL LEU LEU HIS HIS LYS THR MET SER ILE
SEQRES 13 I 437 VAL GLY VAL LEU GLN ASP ASP ALA ASP PRO MET VAL SER
SEQRES 14 I 437 VAL MET LYS MET ASP LYS SER PRO THR GLU SER TYR SER
SEQRES 15 I 437 ASP ILE GLY GLY LEU GLU SER GLN ILE GLN GLU ILE LYS
SEQRES 16 I 437 GLU SER VAL GLU LEU PRO LEU THR HIS PRO GLU LEU TYR
SEQRES 17 I 437 GLU GLU MET GLY ILE LYS PRO PRO LYS GLY VAL ILE LEU
SEQRES 18 I 437 TYR GLY ALA PRO GLY THR GLY LYS THR LEU LEU ALA LYS
SEQRES 19 I 437 ALA VAL ALA ASN GLN THR SER ALA THR PHE LEU ARG ILE
SEQRES 20 I 437 VAL GLY SER GLU LEU ILE GLN LYS TYR LEU GLY ASP GLY
SEQRES 21 I 437 PRO ARG LEU CYS ARG GLN ILE PHE LYS VAL ALA GLY GLU
SEQRES 22 I 437 ASN ALA PRO SER ILE VAL PHE ILE ASP GLU ILE ASP ALA
SEQRES 23 I 437 ILE GLY THR LYS ARG TYR ASP SER ASN SER GLY GLY GLU
SEQRES 24 I 437 ARG GLU ILE GLN ARG THR MET LEU GLU LEU LEU ASN GLN
SEQRES 25 I 437 LEU ASP GLY PHE ASP ASP ARG GLY ASP VAL LYS VAL ILE
SEQRES 26 I 437 MET ALA THR ASN LYS ILE GLU THR LEU ASP PRO ALA LEU
SEQRES 27 I 437 ILE ARG PRO GLY ARG ILE ASP ARG LYS ILE LEU PHE GLU
SEQRES 28 I 437 ASN PRO ASP LEU SER THR LYS LYS LYS ILE LEU GLY ILE
SEQRES 29 I 437 HIS THR SER LYS MET ASN LEU SER GLU ASP VAL ASN LEU
SEQRES 30 I 437 GLU THR LEU VAL THR THR LYS ASP ASP LEU SER GLY ALA
SEQRES 31 I 437 ASP ILE GLN ALA MET CYS THR GLU ALA GLY LEU LEU ALA
SEQRES 32 I 437 LEU ARG GLU ARG ARG MET GLN VAL THR ALA GLU ASP PHE
SEQRES 33 I 437 LYS GLN ALA LYS GLU ARG VAL MET LYS ASN LYS VAL GLU
SEQRES 34 I 437 GLU ASN LEU GLU GLY LEU TYR LEU
SEQRES 1 K 428 MET GLU GLU LEU GLY ILE VAL THR PRO VAL GLU LYS ALA
SEQRES 2 K 428 VAL GLU GLU LYS PRO ALA VAL LYS SER TYR ALA SER LEU
SEQRES 3 K 428 LEU ALA GLN LEU ASN GLY THR VAL ASN ASN ASN SER ALA
SEQRES 4 K 428 LEU SER ASN VAL ASN SER ASP ILE TYR PHE LYS LEU LYS
SEQRES 5 K 428 LYS LEU GLU LYS GLU TYR GLU LEU LEU THR LEU GLN GLU
SEQRES 6 K 428 ASP TYR ILE LYS ASP GLU GLN ARG HIS LEU LYS ARG GLU
SEQRES 7 K 428 LEU LYS ARG ALA GLN GLU GLU VAL LYS ARG ILE GLN SER
SEQRES 8 K 428 VAL PRO LEU VAL ILE GLY GLN PHE LEU GLU PRO ILE ASP
SEQRES 9 K 428 GLN ASN THR GLY ILE VAL SER SER THR THR GLY MET SER
SEQRES 10 K 428 TYR VAL VAL ARG ILE LEU SER THR LEU ASP ARG GLU LEU
SEQRES 11 K 428 LEU LYS PRO SER MET SER VAL ALA LEU HIS ARG HIS SER
SEQRES 12 K 428 ASN ALA LEU VAL ASP ILE LEU PRO PRO ASP SER ASP SER
SEQRES 13 K 428 SER ILE SER VAL MET GLY GLU ASN GLU LYS PRO ASP VAL
SEQRES 14 K 428 THR TYR ALA ASP VAL GLY GLY LEU ASP MET GLN LYS GLN
SEQRES 15 K 428 GLU ILE ARG GLU ALA VAL GLU LEU PRO LEU VAL GLN ALA
SEQRES 16 K 428 ASP LEU TYR GLU GLN ILE GLY ILE ASP PRO PRO ARG GLY
SEQRES 17 K 428 VAL LEU LEU TYR GLY PRO PRO GLY THR GLY LYS THR MET
SEQRES 18 K 428 LEU VAL LYS ALA VAL ALA ASN SER THR LYS ALA ALA PHE
SEQRES 19 K 428 ILE ARG VAL ASN GLY SER GLU PHE VAL HIS LYS TYR LEU
SEQRES 20 K 428 GLY GLU GLY PRO ARG MET VAL ARG ASP VAL PHE ARG LEU
SEQRES 21 K 428 ALA ARG GLU ASN ALA PRO SER ILE ILE PHE ILE ASP GLU
SEQRES 22 K 428 VAL ASP SER ILE ALA THR LYS ARG PHE ASP ALA GLN THR
SEQRES 23 K 428 GLY SER ASP ARG GLU VAL GLN ARG ILE LEU ILE GLU LEU
SEQRES 24 K 428 LEU THR GLN MET ASP GLY PHE ASP GLN SER THR ASN VAL
SEQRES 25 K 428 LYS VAL ILE MET ALA THR ASN ARG ALA ASP THR LEU ASP
SEQRES 26 K 428 PRO ALA LEU LEU ARG PRO GLY ARG LEU ASP ARG LYS ILE
SEQRES 27 K 428 GLU PHE PRO SER LEU ARG ASP ARG ARG GLU ARG ARG LEU
SEQRES 28 K 428 ILE PHE GLY THR ILE ALA SER LYS MET SER LEU ALA PRO
SEQRES 29 K 428 GLU ALA ASP LEU ASP SER LEU ILE ILE ARG ASN ASP SER
SEQRES 30 K 428 LEU SER GLY ALA VAL ILE ALA ALA ILE MET GLN GLU ALA
SEQRES 31 K 428 GLY LEU ARG ALA VAL ARG LYS ASN ARG TYR VAL ILE LEU
SEQRES 32 K 428 GLN SER ASP LEU GLU GLU ALA TYR ALA THR GLN VAL LYS
SEQRES 33 K 428 THR ASP ASN THR VAL ASP LYS PHE ASP PHE TYR LYS
SEQRES 1 L 437 MET SER GLU GLU GLN ASP PRO LEU LEU ALA GLY LEU GLY
SEQRES 2 L 437 GLU THR SER GLY ASP ASN HIS THR GLN GLN SER HIS GLU
SEQRES 3 L 437 GLN GLN PRO GLU GLN PRO GLN GLU THR GLU GLU HIS HIS
SEQRES 4 L 437 GLU GLU GLU PRO SER ARG VAL ASP PRO GLU GLN GLU ALA
SEQRES 5 L 437 HIS ASN LYS ALA LEU ASN GLN PHE LYS ARG LYS LEU LEU
SEQRES 6 L 437 GLU HIS ARG ARG TYR ASP ASP GLN LEU LYS GLN ARG ARG
SEQRES 7 L 437 GLN ASN ILE ARG ASP LEU GLU LYS LEU TYR ASP LYS THR
SEQRES 8 L 437 GLU ASN ASP ILE LYS ALA LEU GLN SER ILE GLY GLN LEU
SEQRES 9 L 437 ILE GLY GLU VAL MET LYS GLU LEU SER GLU GLU LYS TYR
SEQRES 10 L 437 ILE VAL LYS ALA SER SER GLY PRO ARG TYR ILE VAL GLY
SEQRES 11 L 437 VAL ARG ASN SER VAL ASP ARG SER LYS LEU LYS LYS GLY
SEQRES 12 L 437 VAL ARG VAL THR LEU ASP ILE THR THR LEU THR ILE MET
SEQRES 13 L 437 ARG ILE LEU PRO ARG GLU THR ASP PRO LEU VAL TYR ASN
SEQRES 14 L 437 MET THR SER PHE GLU GLN GLY GLU ILE THR PHE ASP GLY
SEQRES 15 L 437 ILE GLY GLY LEU THR GLU GLN ILE ARG GLU LEU ARG GLU
SEQRES 16 L 437 VAL ILE GLU LEU PRO LEU LYS ASN PRO GLU ILE PHE GLN
SEQRES 17 L 437 ARG VAL GLY ILE LYS PRO PRO LYS GLY VAL LEU LEU TYR
SEQRES 18 L 437 GLY PRO PRO GLY THR GLY LYS THR LEU LEU ALA LYS ALA
SEQRES 19 L 437 VAL ALA ALA THR ILE GLY ALA ASN PHE ILE PHE SER PRO
SEQRES 20 L 437 ALA SER GLY ILE VAL ASP LYS TYR ILE GLY GLU SER ALA
SEQRES 21 L 437 ARG ILE ILE ARG GLU MET PHE ALA TYR ALA LYS GLU HIS
SEQRES 22 L 437 GLU PRO CYS ILE ILE PHE MET ASP GLU VAL ASP ALA ILE
SEQRES 23 L 437 GLY GLY ARG ARG PHE SER GLU GLY THR SER ALA ASP ARG
SEQRES 24 L 437 GLU ILE GLN ARG THR LEU MET GLU LEU LEU THR GLN MET
SEQRES 25 L 437 ASP GLY PHE ASP ASN LEU GLY GLN THR LYS ILE ILE MET
SEQRES 26 L 437 ALA THR ASN ARG PRO ASP THR LEU ASP PRO ALA LEU LEU
SEQRES 27 L 437 ARG PRO GLY ARG LEU ASP ARG LYS VAL GLU ILE PRO LEU
SEQRES 28 L 437 PRO ASN GLU ALA GLY ARG LEU GLU ILE PHE LYS ILE HIS
SEQRES 29 L 437 THR ALA LYS VAL LYS LYS THR GLY GLU PHE ASP PHE GLU
SEQRES 30 L 437 ALA ALA VAL LYS MET SER ASP GLY PHE ASN GLY ALA ASP
SEQRES 31 L 437 ILE ARG ASN CYS ALA THR GLU ALA GLY PHE PHE ALA ILE
SEQRES 32 L 437 ARG ASP ASP ARG ASP HIS ILE ASN PRO ASP ASP LEU MET
SEQRES 33 L 437 LYS ALA VAL ARG LYS VAL ALA GLU VAL LYS LYS LEU GLU
SEQRES 34 L 437 GLY THR ILE GLU TYR GLN LYS LEU
SEQRES 1 M 434 MET ALA THR LEU GLU GLU LEU ASP ALA GLN THR LEU PRO
SEQRES 2 M 434 GLY ASP ASP GLU LEU ASP GLN GLU ILE LEU ASN LEU SER
SEQRES 3 M 434 THR GLN GLU LEU GLN THR ARG ALA LYS LEU LEU ASP ASN
SEQRES 4 M 434 GLU ILE ARG ILE PHE ARG SER GLU LEU GLN ARG LEU SER
SEQRES 5 M 434 HIS GLU ASN ASN VAL MET LEU GLU LYS ILE LYS ASP ASN
SEQRES 6 M 434 LYS GLU LYS ILE LYS ASN ASN ARG GLN LEU PRO TYR LEU
SEQRES 7 M 434 VAL ALA ASN VAL VAL GLU VAL MET ASP MET ASN GLU ILE
SEQRES 8 M 434 GLU ASP LYS GLU ASN SER GLU SER THR THR GLN GLY GLY
SEQRES 9 M 434 ASN VAL ASN LEU ASP ASN THR ALA VAL GLY LYS ALA ALA
SEQRES 10 M 434 VAL VAL LYS THR SER SER ARG GLN THR VAL PHE LEU PRO
SEQRES 11 M 434 MET VAL GLY LEU VAL ASP PRO ASP LYS LEU LYS PRO ASN
SEQRES 12 M 434 ASP LEU VAL GLY VAL ASN LYS ASP SER TYR LEU ILE LEU
SEQRES 13 M 434 ASP THR LEU PRO SER GLU PHE ASP SER ARG VAL LYS ALA
SEQRES 14 M 434 MET GLU VAL ASP GLU LYS PRO THR GLU THR TYR SER ASP
SEQRES 15 M 434 VAL GLY GLY LEU ASP LYS GLN ILE GLU GLU LEU VAL GLU
SEQRES 16 M 434 ALA ILE VAL LEU PRO MET LYS ARG ALA ASP LYS PHE LYS
SEQRES 17 M 434 ASP MET GLY ILE ARG ALA PRO LYS GLY ALA LEU MET TYR
SEQRES 18 M 434 GLY PRO PRO GLY THR GLY LYS THR LEU LEU ALA ARG ALA
SEQRES 19 M 434 CYS ALA ALA GLN THR ASN ALA THR PHE LEU LYS LEU ALA
SEQRES 20 M 434 ALA PRO GLN LEU VAL GLN MET TYR ILE GLY GLU GLY ALA
SEQRES 21 M 434 LYS LEU VAL ARG ASP ALA PHE ALA LEU ALA LYS GLU LYS
SEQRES 22 M 434 ALA PRO THR ILE ILE PHE ILE ASP GLU LEU ASP ALA ILE
SEQRES 23 M 434 GLY THR LYS ARG PHE ASP SER GLU LYS SER GLY ASP ARG
SEQRES 24 M 434 GLU VAL GLN ARG THR MET LEU GLU LEU LEU ASN GLN LEU
SEQRES 25 M 434 ASP GLY PHE SER SER ASP ASP ARG VAL LYS VAL LEU ALA
SEQRES 26 M 434 ALA THR ASN ARG VAL ASP VAL LEU ASP PRO ALA LEU LEU
SEQRES 27 M 434 ARG SER GLY ARG LEU ASP ARG LYS ILE GLU PHE PRO LEU
SEQRES 28 M 434 PRO SER GLU ASP SER ARG ALA GLN ILE LEU GLN ILE HIS
SEQRES 29 M 434 SER ARG LYS MET THR THR ASP ASP ASP ILE ASN TRP GLN
SEQRES 30 M 434 GLU LEU ALA ARG SER THR ASP GLU PHE ASN GLY ALA GLN
SEQRES 31 M 434 LEU LYS ALA VAL THR VAL GLU ALA GLY MET ILE ALA LEU
SEQRES 32 M 434 ARG ASN GLY GLN SER SER VAL LYS HIS GLU ASP PHE VAL
SEQRES 33 M 434 GLU GLY ILE SER GLU VAL GLN ALA ARG LYS SER LYS SER
SEQRES 34 M 434 VAL SER PHE TYR ALA
SEQRES 1 J 405 MET THR ALA ALA VAL THR SER SER ASN ILE VAL LEU GLU
SEQRES 2 J 405 THR HIS GLU SER GLY ILE LYS PRO TYR PHE GLU GLN LYS
SEQRES 3 J 405 ILE GLN GLU THR GLU LEU LYS ILE ARG SER LYS THR GLU
SEQRES 4 J 405 ASN VAL ARG ARG LEU GLU ALA GLN ARG ASN ALA LEU ASN
SEQRES 5 J 405 ASP LYS VAL ARG PHE ILE LYS ASP GLU LEU ARG LEU LEU
SEQRES 6 J 405 GLN GLU PRO GLY SER TYR VAL GLY GLU VAL ILE LYS ILE
SEQRES 7 J 405 VAL SER ASP LYS LYS VAL LEU VAL LYS VAL GLN PRO GLU
SEQRES 8 J 405 GLY LYS TYR ILE VAL ASP VAL ALA LYS ASP ILE ASN VAL
SEQRES 9 J 405 LYS ASP LEU LYS ALA SER GLN ARG VAL CYS LEU ARG SER
SEQRES 10 J 405 ASP SER TYR MET LEU HIS LYS VAL LEU GLU ASN LYS ALA
SEQRES 11 J 405 ASP PRO LEU VAL SER LEU MET MET VAL GLU LYS VAL PRO
SEQRES 12 J 405 ASP SER THR TYR ASP MET VAL GLY GLY LEU THR LYS GLN
SEQRES 13 J 405 ILE LYS GLU ILE LYS GLU VAL ILE GLU LEU PRO VAL LYS
SEQRES 14 J 405 HIS PRO GLU LEU PHE GLU SER LEU GLY ILE ALA GLN PRO
SEQRES 15 J 405 LYS GLY VAL ILE LEU TYR GLY PRO PRO GLY THR GLY LYS
SEQRES 16 J 405 THR LEU LEU ALA ARG ALA VAL ALA HIS HIS THR ASP CYS
SEQRES 17 J 405 LYS PHE ILE ARG VAL SER GLY ALA GLU LEU VAL GLN LYS
SEQRES 18 J 405 TYR ILE GLY GLU GLY SER ARG MET VAL ARG GLU LEU PHE
SEQRES 19 J 405 VAL MET ALA ARG GLU HIS ALA PRO SER ILE ILE PHE MET
SEQRES 20 J 405 ASP GLU ILE ASP SER ILE GLY SER THR ARG VAL GLU GLY
SEQRES 21 J 405 SER GLY GLY GLY ASP SER GLU VAL GLN ARG THR MET LEU
SEQRES 22 J 405 GLU LEU LEU ASN GLN LEU ASP GLY PHE GLU THR SER LYS
SEQRES 23 J 405 ASN ILE LYS ILE ILE MET ALA THR ASN ARG LEU ASP ILE
SEQRES 24 J 405 LEU ASP PRO ALA LEU LEU ARG PRO GLY ARG ILE ASP ARG
SEQRES 25 J 405 LYS ILE GLU PHE PRO PRO PRO SER VAL ALA ALA ARG ALA
SEQRES 26 J 405 GLU ILE LEU ARG ILE HIS SER ARG LYS MET ASN LEU THR
SEQRES 27 J 405 ARG GLY ILE ASN LEU ARG LYS VAL ALA GLU LYS MET ASN
SEQRES 28 J 405 GLY CYS SER GLY ALA ASP VAL LYS GLY VAL CYS THR GLU
SEQRES 29 J 405 ALA GLY MET TYR ALA LEU ARG GLU ARG ARG ILE HIS VAL
SEQRES 30 J 405 THR GLN GLU ASP PHE GLU LEU ALA VAL GLY LYS VAL MET
SEQRES 31 J 405 ASN LYS ASN GLN GLU THR ALA ILE SER VAL ALA LYS LEU
SEQRES 32 J 405 PHE LYS
HET MG H 501 1
HET ATP H 502 31
HET ATP I 501 31
HET MG I 502 1
HET ATP K 501 31
HET MG K 502 1
HET ATP L 501 31
HET MG L 502 1
HET ATP M 501 31
HET MG M 502 1
HET ADP J 501 27
HET MG J 502 1
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 35 MG 6(MG 2+)
FORMUL 36 ATP 5(C10 H16 N5 O13 P3)
FORMUL 45 ADP C10 H15 N5 O10 P2
HELIX 1 AA1 GLY a 2 HIS a 6 5 5
HELIX 2 AA2 LEU a 16 ASN a 27 1 12
HELIX 3 AA3 PRO a 77 GLY a 100 1 24
HELIX 4 AA4 PRO a 104 ARG a 122 1 19
HELIX 5 AA5 LYS a 165 LYS a 181 1 17
HELIX 6 AA6 SER a 189 GLY a 206 1 18
HELIX 7 AA7 SER a 228 GLN a 242 1 15
HELIX 8 AA8 GLY b 19 GLY b 31 1 13
HELIX 9 AA9 MET b 78 SER b 96 1 19
HELIX 10 AB1 PRO b 106 SER b 124 1 19
HELIX 11 AB2 GLY b 167 TRP b 179 1 13
HELIX 12 AB3 GLU b 184 SER b 199 1 16
HELIX 13 AB4 THR b 239 LEU b 247 1 9
HELIX 14 AB5 SER c 2 ASP c 6 5 5
HELIX 15 AB6 LEU c 18 ALA c 31 1 14
HELIX 16 AB7 LEU c 79 ASN c 102 1 24
HELIX 17 AB8 PRO c 106 GLY c 120 1 15
HELIX 18 AB9 ASN c 167 TYR c 179 1 13
HELIX 19 AC1 LYS c 184 THR c 200 1 17
HELIX 20 AC2 LYS c 235 THR c 241 1 7
HELIX 21 AC3 ILE d 15 GLY d 28 1 14
HELIX 22 AC4 LEU d 76 GLU d 99 1 24
HELIX 23 AC5 THR d 103 ARG d 117 1 15
HELIX 24 AC6 LYS d 167 TYR d 177 1 11
HELIX 25 AC7 THR d 185 LEU d 198 1 14
HELIX 26 AC8 SER d 223 GLN d 239 1 17
HELIX 27 AC9 LEU e 13 GLY e 26 1 14
HELIX 28 AD1 GLU e 52 ILE e 56 5 5
HELIX 29 AD2 LEU e 73 TYR e 95 1 23
HELIX 30 AD3 ASN e 100 ASP e 110 1 11
HELIX 31 AD4 LEU e 111 ARG e 114 5 4
HELIX 32 AD5 GLY e 167 TRP e 179 1 13
HELIX 33 AD6 THR e 184 MET e 200 1 17
HELIX 34 AD7 ASP e 224 ALA e 241 1 18
HELIX 35 AD8 LEU f 18 LYS f 29 1 12
HELIX 36 AD9 LEU f 76 ASN f 99 1 24
HELIX 37 AE1 ALA f 103 SER f 121 1 19
HELIX 38 AE2 SER f 164 LYS f 180 1 17
HELIX 39 AE3 ASN f 184 LEU f 200 1 17
HELIX 40 AE4 ASP f 225 ALA f 230 5 6
HELIX 41 AE5 ASN g 17 ASN g 29 1 13
HELIX 42 AE6 LEU g 77 TYR g 99 1 23
HELIX 43 AE7 PRO g 104 ALA g 118 1 15
HELIX 44 AE8 HIS g 119 LEU g 121 5 3
HELIX 45 AE9 GLY g 164 HIS g 178 1 15
HELIX 46 AF1 SER g 184 HIS g 200 1 17
HELIX 47 AF2 LYS g 228 LYS g 241 1 14
HELIX 48 AF3 SER h 48 GLY h 71 1 24
HELIX 49 AF4 SER h 74 TYR h 87 1 14
HELIX 50 AF5 GLY h 130 PHE h 133 5 4
HELIX 51 AF6 ILE h 134 PHE h 142 1 9
HELIX 52 AF7 SER h 147 ASP h 166 1 20
HELIX 53 AF8 TYR h 189 TYR h 193 5 5
HELIX 54 AF9 THR i 48 SER i 71 1 24
HELIX 55 AG1 ARG i 75 LYS i 89 1 15
HELIX 56 AG2 SER i 131 TRP i 142 1 12
HELIX 57 AG3 THR i 147 ASP i 166 1 20
HELIX 58 AG4 LEU j 55 GLU j 78 1 24
HELIX 59 AG5 GLU j 82 TYR j 95 1 14
HELIX 60 AG6 ALA j 141 TYR j 153 1 13
HELIX 61 AG7 ASP j 161 ASP j 175 1 15
HELIX 62 AG8 GLY k 51 ASP k 72 1 22
HELIX 63 AG9 SER k 76 SER k 94 1 19
HELIX 64 AH1 TYR k 135 PHE k 141 1 7
HELIX 65 AH2 SER k 142 TYR k 148 1 7
HELIX 66 AH3 THR k 153 MET k 172 1 20
HELIX 67 AH4 GLY l 48 LYS l 71 1 24
HELIX 68 AH5 SER l 75 TYR l 90 1 16
HELIX 69 AH6 GLY l 132 ASN l 143 1 12
HELIX 70 AH7 SER l 149 ASP l 168 1 20
HELIX 71 AH8 VAL l 193 GLY l 205 1 13
HELIX 72 AH9 PHE m 57 HIS m 79 1 23
HELIX 73 AI1 SER m 85 LYS m 100 1 16
HELIX 74 AI2 ARG m 101 PHE m 103 5 3
HELIX 75 AI3 ALA m 142 ASN m 155 1 14
HELIX 76 AI4 SER m 176 HIS m 195 1 20
HELIX 77 AI5 ILE n 57 TYR n 76 1 20
HELIX 78 AI6 ASN n 78 GLU n 84 1 7
HELIX 79 AI7 GLU n 88 LYS n 106 1 19
HELIX 80 AI8 GLY n 145 HIS n 149 5 5
HELIX 81 AI9 ALA n 151 LYS n 157 1 7
HELIX 82 AJ1 ARG n 161 ILE n 165 5 5
HELIX 83 AJ2 THR n 169 ASP n 188 1 20
HELIX 84 AJ3 ASP n 220 ASP n 224 5 5
HELIX 85 AJ4 TYR A 3 ILE A 7 1 5
HELIX 86 AJ5 LEU A 16 LYS A 24 1 9
HELIX 87 AJ6 PRO A 77 GLY A 100 1 24
HELIX 88 AJ7 PRO A 104 ARG A 122 1 19
HELIX 89 AJ8 LYS A 165 SER A 180 1 16
HELIX 90 AJ9 SER A 189 GLY A 206 1 18
HELIX 91 AK1 SER A 228 GLU A 241 1 14
HELIX 92 AK2 LEU B 18 GLY B 31 1 14
HELIX 93 AK3 MET B 78 THR B 95 1 18
HELIX 94 AK4 PRO B 106 SER B 124 1 19
HELIX 95 AK5 SER B 168 TRP B 179 1 12
HELIX 96 AK6 GLU B 184 VAL B 200 1 17
HELIX 97 AK7 THR B 239 LEU B 247 1 9
HELIX 98 AK8 SER C 2 ASP C 6 1 5
HELIX 99 AK9 LEU C 18 ALA C 31 1 14
HELIX 100 AL1 LEU C 79 ASN C 102 1 24
HELIX 101 AL2 PRO C 106 HIS C 124 1 19
HELIX 102 AL3 ASN C 167 TYR C 179 1 13
HELIX 103 AL4 LYS C 184 THR C 200 1 17
HELIX 104 AL5 PHE D 16 GLY D 28 1 13
HELIX 105 AL6 LEU D 76 GLU D 99 1 24
HELIX 106 AL7 THR D 103 SER D 121 1 19
HELIX 107 AL8 ASN D 165 TYR D 177 1 13
HELIX 108 AL9 THR D 185 LEU D 198 1 14
HELIX 109 AM1 SER D 223 GLU D 240 1 18
HELIX 110 AM2 LEU E 13 GLY E 26 1 14
HELIX 111 AM3 GLU E 52 ILE E 56 5 5
HELIX 112 AM4 LEU E 73 TYR E 95 1 23
HELIX 113 AM5 ASN E 100 ARG E 114 1 15
HELIX 114 AM6 GLY E 167 TRP E 179 1 13
HELIX 115 AM7 THR E 184 VAL E 199 1 16
HELIX 116 AM8 ASP E 224 GLU E 242 1 19
HELIX 117 AM9 LEU F 18 GLY F 31 1 14
HELIX 118 AN1 LEU F 76 VAL F 97 1 22
HELIX 119 AN2 ALA F 103 SER F 121 1 19
HELIX 120 AN3 SER F 164 THR F 174 1 11
HELIX 121 AN4 THR F 174 ILE F 179 1 6
HELIX 122 AN5 ASN F 184 SER F 197 1 14
HELIX 123 AN6 ALA F 228 ILE F 233 1 6
HELIX 124 AN7 GLY G 3 SER G 7 1 5
HELIX 125 AN8 ASN G 17 GLY G 30 1 14
HELIX 126 AN9 LEU G 77 LYS G 100 1 24
HELIX 127 AO1 PRO G 104 HIS G 119 1 16
HELIX 128 AO2 ARG G 165 LYS G 174 1 10
HELIX 129 AO3 SER G 184 ALA G 199 1 16
HELIX 130 AO4 GLY G 229 LYS G 241 1 13
HELIX 131 AO5 SER 1 48 SER 1 68 1 21
HELIX 132 AO6 SER 1 74 ASN 1 89 1 16
HELIX 133 AO7 GLY 1 130 PHE 1 142 1 13
HELIX 134 AO8 SER 1 147 ASP 1 166 1 20
HELIX 135 AO9 TYR 1 189 LEU 1 196 1 8
HELIX 136 AP1 THR 2 48 SER 2 71 1 24
HELIX 137 AP2 ARG 2 75 LYS 2 89 1 15
HELIX 138 AP3 GLY 2 130 TRP 2 142 1 13
HELIX 139 AP4 THR 2 147 ASP 2 166 1 20
HELIX 140 AP5 PRO 3 3 GLY 3 8 1 6
HELIX 141 AP6 LEU 3 55 GLU 3 78 1 24
HELIX 142 AP7 GLU 3 82 GLU 3 96 1 15
HELIX 143 AP8 ALA 3 141 TYR 3 153 1 13
HELIX 144 AP9 GLU 3 158 ASP 3 175 1 18
HELIX 145 AQ1 GLY 4 51 ASP 4 72 1 22
HELIX 146 AQ2 SER 4 76 SER 4 94 1 19
HELIX 147 AQ3 SER 4 136 TYR 4 148 1 13
HELIX 148 AQ4 THR 4 153 MET 4 172 1 20
HELIX 149 AQ5 GLY 5 48 GLU 5 70 1 23
HELIX 150 AQ6 SER 5 75 TYR 5 90 1 16
HELIX 151 AQ7 GLY 5 130 GLY 5 132 5 3
HELIX 152 AQ8 GLN 5 133 ASN 5 143 1 11
HELIX 153 AQ9 SER 5 149 ASP 5 168 1 20
HELIX 154 AR1 VAL 5 193 GLU 5 203 1 11
HELIX 155 AR2 PHE 6 57 HIS 6 79 1 23
HELIX 156 AR3 SER 6 85 LYS 6 100 1 16
HELIX 157 AR4 ALA 6 142 VAL 6 154 1 13
HELIX 158 AR5 SER 6 176 HIS 6 195 1 20
HELIX 159 AR6 ILE 7 57 TYR 7 76 1 20
HELIX 160 AR7 GLU 7 88 LYS 7 106 1 19
HELIX 161 AR8 GLY 7 145 HIS 7 149 5 5
HELIX 162 AR9 MET 7 150 VAL 7 159 1 10
HELIX 163 AS1 THR 7 169 ASP 7 188 1 20
HELIX 164 AS2 ASP 7 220 ASP 7 224 5 5
HELIX 165 AS3 ALA H 43 ALA H 47 1 5
HELIX 166 AS4 LYS H 48 GLY H 68 1 21
HELIX 167 AS5 ALA H 77 HIS H 80 5 4
HELIX 168 AS6 LEU H 81 GLY H 92 1 12
HELIX 169 AS7 ASP H 216 VAL H 225 1 10
HELIX 170 AS8 VAL H 225 SER H 231 1 7
HELIX 171 AS9 GLU H 233 GLY H 239 1 7
HELIX 172 AT1 THR H 257 THR H 267 1 11
HELIX 173 AT2 GLY H 285 LYS H 301 1 17
HELIX 174 AT3 GLY H 325 ASP H 341 1 17
HELIX 175 AT4 GLU H 383 SER H 393 1 11
HELIX 176 AT5 ARG H 403 CYS H 411 1 9
HELIX 177 AT6 THR H 415 ARG H 420 1 6
HELIX 178 AT7 ARG H 420 ARG H 434 1 15
HELIX 179 AT8 THR H 439 LYS H 456 1 18
HELIX 180 AT9 ARG I 54 SER I 77 1 24
HELIX 181 AU1 PHE I 85 GLY I 101 1 17
HELIX 182 AU2 PRO I 166 LYS I 172 1 7
HELIX 183 AU3 LEU I 187 ILE I 191 5 5
HELIX 184 AU4 GLU I 193 VAL I 198 1 6
HELIX 185 AU5 GLU I 199 HIS I 204 1 6
HELIX 186 AU6 HIS I 204 MET I 211 1 8
HELIX 187 AU7 GLY I 228 THR I 240 1 13
HELIX 188 AU8 GLY I 258 ASN I 274 1 17
HELIX 189 AU9 ASP I 285 THR I 289 5 5
HELIX 190 AV1 GLY I 297 ASP I 314 1 18
HELIX 191 AV2 SER I 356 THR I 366 1 11
HELIX 192 AV3 ASN I 376 LYS I 384 1 9
HELIX 193 AV4 SER I 388 THR I 397 1 10
HELIX 194 AV5 GLU I 398 ARG I 407 1 10
HELIX 195 AV6 THR I 412 GLU I 430 1 19
HELIX 196 AV7 SER K 41 TYR K 58 1 18
HELIX 197 AV8 TYR K 58 SER K 91 1 34
HELIX 198 AV9 LYS K 181 VAL K 188 1 8
HELIX 199 AW1 VAL K 188 GLN K 194 1 7
HELIX 200 AW2 ALA K 195 GLY K 202 1 8
HELIX 201 AW3 GLY K 218 LYS K 231 1 14
HELIX 202 AW4 GLY K 248 ASN K 264 1 17
HELIX 203 AW5 THR K 286 PHE K 306 1 21
HELIX 204 AW6 ARG K 320 LEU K 324 5 5
HELIX 205 AW7 ASP K 325 ARG K 330 1 6
HELIX 206 AW8 ASP K 345 MET K 360 1 16
HELIX 207 AW9 ASP K 369 ASN K 375 1 7
HELIX 208 AX1 GLY K 380 ASN K 398 1 19
HELIX 209 AX2 LEU K 403 ALA K 412 1 10
HELIX 210 AX3 LEU L 57 ARG L 82 1 26
HELIX 211 AX4 ARG L 82 GLN L 99 1 18
HELIX 212 AX5 PRO L 165 MET L 170 1 6
HELIX 213 AX6 LEU L 186 ILE L 197 1 12
HELIX 214 AX7 ILE L 197 ASN L 203 1 7
HELIX 215 AX8 PRO L 204 GLY L 211 1 8
HELIX 216 AX9 GLY L 227 THR L 238 1 12
HELIX 217 AY1 SER L 249 ILE L 251 5 3
HELIX 218 AY2 GLY L 257 HIS L 273 1 17
HELIX 219 AY3 SER L 296 ASP L 313 1 18
HELIX 220 AY4 ARG L 357 VAL L 368 1 12
HELIX 221 AY5 ASP L 375 MET L 382 1 8
HELIX 222 AY6 ASN L 387 ARG L 392 1 6
HELIX 223 AY7 ASN L 393 GLY L 399 1 7
HELIX 224 AY8 PHE L 400 ASP L 406 1 7
HELIX 225 AY9 ASN L 411 LYS L 427 1 17
HELIX 226 AZ1 GLN M 28 LYS M 35 1 8
HELIX 227 AZ2 LYS M 35 GLN M 74 1 40
HELIX 228 AZ3 ASP M 164 GLU M 171 1 8
HELIX 229 AZ4 LEU M 186 ILE M 197 1 12
HELIX 230 AZ5 VAL M 198 ARG M 203 1 6
HELIX 231 AZ6 ASP M 205 GLY M 211 1 7
HELIX 232 AZ7 GLY M 227 THR M 239 1 13
HELIX 233 AZ8 PRO M 249 LEU M 251 5 3
HELIX 234 AZ9 GLY M 259 LYS M 273 1 15
HELIX 235 BA1 GLY M 297 GLN M 311 1 15
HELIX 236 BA2 SER M 353 ARG M 366 1 14
HELIX 237 BA3 ASN M 375 THR M 383 1 9
HELIX 238 BA4 ASN M 387 GLY M 406 1 20
HELIX 239 BA5 GLU M 413 GLY M 418 1 6
HELIX 240 BA6 THR J 14 ILE J 19 1 6
HELIX 241 BA7 PHE J 23 LEU J 65 1 43
HELIX 242 BA8 ASP J 131 LYS J 141 1 11
HELIX 243 BA9 LEU J 153 ILE J 164 1 12
HELIX 244 BB1 GLU J 165 HIS J 170 1 6
HELIX 245 BB2 HIS J 170 GLY J 178 1 9
HELIX 246 BB3 GLY J 194 THR J 206 1 13
HELIX 247 BB4 VAL J 230 HIS J 240 1 11
HELIX 248 BB5 GLY J 264 ASN J 277 1 14
HELIX 249 BB6 SER J 320 SER J 332 1 13
HELIX 250 BB7 ASN J 342 MET J 350 1 9
HELIX 251 BB8 ALA J 356 ARG J 373 1 18
HELIX 252 BB9 GLU J 380 ALA J 397 1 18
SHEET 1 A 5 ALA a 159 THR a 162 0
SHEET 2 A 5 SER a 33 ARG a 37 -1
SHEET 3 A 5 CYS a 41 GLN a 47 -1
SHEET 4 A 5 LEU a 214 THR a 220 -1
SHEET 5 A 5 LYS a 223 THR a 226 -1
SHEET 1 B 5 ILE a 63 CYS a 65 0
SHEET 2 B 5 GLY a 71 GLY a 76 -1
SHEET 3 B 5 VAL a 130 VAL a 137 -1
SHEET 4 B 5 PRO a 143 THR a 148 -1
SHEET 5 B 5 TYR a 154 GLY a 156 -1
SHEET 1 C 5 ALA b 161 ILE b 164 0
SHEET 2 C 5 SER b 34 LYS b 38 -1
SHEET 3 C 5 VAL b 43 GLU b 48 -1
SHEET 4 C 5 ILE b 209 ILE b 214 -1
SHEET 5 C 5 PHE b 235 LYS b 237 -1
SHEET 1 D 5 TYR b 156 PRO b 158 0
SHEET 2 D 5 PHE b 145 VAL b 150 -1
SHEET 3 D 5 VAL b 132 HIS b 139 -1
SHEET 4 D 5 ILE b 71 GLY b 77 -1
SHEET 5 D 5 VAL b 64 THR b 68 -1
SHEET 1 E 4 ALA c 161 VAL c 164 0
SHEET 2 E 4 ALA c 34 MET c 38 -1
SHEET 3 E 4 ILE c 43 GLU c 48 -1
SHEET 4 E 4 LEU c 210 ILE c 215 -1
SHEET 1 F 5 TYR c 156 GLY c 158 0
SHEET 2 F 5 TYR c 145 SER c 150 -1
SHEET 3 F 5 VAL c 132 TYR c 139 -1
SHEET 4 F 5 ILE c 72 GLY c 78 -1
SHEET 5 F 5 LEU c 65 ASN c 69 -1
SHEET 1 G 5 ALA d 159 ILE d 162 0
SHEET 2 G 5 ALA d 31 LYS d 35 -1
SHEET 3 G 5 CYS d 39 GLU d 45 -1
SHEET 4 G 5 ILE d 208 LYS d 214 -1
SHEET 5 G 5 ASP d 218 ALA d 221 -1
SHEET 1 H 5 VAL d 62 LYS d 64 0
SHEET 2 H 5 VAL d 69 GLY d 75 -1
SHEET 3 H 5 VAL d 129 PHE d 136 -1
SHEET 4 H 5 PRO d 143 THR d 148 -1
SHEET 5 H 5 TYR d 154 SER d 156 -1
SHEET 1 I 5 ALA e 161 ILE e 164 0
SHEET 2 I 5 ALA e 29 ILE e 32 -1
SHEET 3 I 5 VAL e 38 GLU e 43 -1
SHEET 4 I 5 ALA e 209 THR e 215 -1
SHEET 5 I 5 GLY e 219 ILE e 222 -1
SHEET 1 J 4 TYR e 145 ALA e 150 0
SHEET 2 J 4 VAL e 132 HIS e 139 -1
SHEET 3 J 4 ILE e 66 GLY e 72 -1
SHEET 4 J 4 ILE e 59 ASP e 63 -1
SHEET 1 K 5 GLY f 157 ILE f 160 0
SHEET 2 K 5 THR f 34 ARG f 38 -1
SHEET 3 K 5 HIS f 42 LEU f 48 -1
SHEET 4 K 5 LEU f 210 GLY f 216 -1
SHEET 5 K 5 THR f 222 TYR f 224 -1
SHEET 1 L 5 ILE f 62 LYS f 64 0
SHEET 2 L 5 GLY f 70 GLY f 75 -1
SHEET 3 L 5 VAL f 129 ASP f 137 -1
SHEET 4 L 5 GLY f 140 PHE f 146 -1
SHEET 5 L 5 VAL f 152 GLU f 154 -1
SHEET 1 M 4 GLY g 158 THR g 161 0
SHEET 2 M 4 SER g 33 LYS g 37 -1
SHEET 3 M 4 GLY g 41 LEU g 49 -1
SHEET 4 M 4 PHE g 208 SER g 216 -1
SHEET 1 N 5 ILE g 63 VAL g 66 0
SHEET 2 N 5 ILE g 70 GLY g 76 -1
SHEET 3 N 5 VAL g 130 VAL g 137 -1
SHEET 4 N 5 ALA g 142 GLU g 148 -1
SHEET 5 N 5 SER g 152 GLY g 155 -1
SHEET 1 O 5 TYR h 124 GLY h 128 0
SHEET 2 O 5 SER h 2 THR h 7 -1
SHEET 3 O 5 VAL h 12 ALA h 16 -1
SHEET 4 O 5 ILE h 173 LEU h 178 -1
SHEET 5 O 5 VAL h 183 PHE h 188 -1
SHEET 1 P 5 LEU h 34 ARG h 36 0
SHEET 2 P 5 ILE h 41 GLY h 47 -1
SHEET 3 P 5 ALA h 95 TYR h 102 -1
SHEET 4 P 5 GLY h 108 ILE h 113 -1
SHEET 5 P 5 HIS h 120 LEU h 122 -1
SHEET 1 Q 2 THR h 20 THR h 22 0
SHEET 2 Q 2 TYR h 25 ASN h 28 -1
SHEET 1 R 4 TYR i 124 LEU i 127 0
SHEET 2 R 4 ILE i 3 PHE i 8 -1
SHEET 3 R 4 GLY i 11 ASP i 17 -1
SHEET 4 R 4 VAL i 173 GLU i 179 -1
SHEET 1 S 5 SER i 118 VAL i 121 0
SHEET 2 S 5 SER i 108 HIS i 114 -1
SHEET 3 S 5 ALA i 96 VAL i 103 -1
SHEET 4 S 5 ILE i 41 GLY i 47 -1
SHEET 5 S 5 LEU i 34 SER i 38 -1
SHEET 1 T 5 PHE j 135 GLY j 139 0
SHEET 2 T 5 ILE j 10 GLY j 16 -1
SHEET 3 T 5 CYS j 19 ASP j 25 -1
SHEET 4 T 5 ALA j 184 LYS j 190 -1
SHEET 5 T 5 VAL j 194 LEU j 199 -1
SHEET 1 U 4 ILE j 42 TYR j 45 0
SHEET 2 U 4 VAL j 48 GLY j 51 -1
SHEET 3 U 4 VAL j 107 ILE j 111 -1
SHEET 4 U 4 PRO j 118 ALA j 121 -1
SHEET 1 V 2 LEU j 28 SER j 30 0
SHEET 2 V 2 LEU j 33 SER j 36 -1
SHEET 1 W 5 TYR k 130 ALA k 132 0
SHEET 2 W 5 ILE k 4 VAL k 9 -1
SHEET 3 W 5 SER k 12 SER k 18 -1
SHEET 4 W 5 VAL k 179 ASP k 185 -1
SHEET 5 W 5 GLY k 188 ARG k 190 -1
SHEET 1 X 5 THR k 124 GLU k 127 0
SHEET 2 X 5 LYS k 113 ASP k 120 -1
SHEET 3 X 5 VAL k 100 ASP k 108 -1
SHEET 4 X 5 THR k 42 GLY k 48 -1
SHEET 5 X 5 THR k 35 SER k 39 -1
SHEET 1 Y 5 ILE l 126 GLY l 130 0
SHEET 2 Y 5 THR l 2 PHE l 8 -1
SHEET 3 Y 5 GLY l 11 VAL l 16 -1
SHEET 4 Y 5 SER l 174 VAL l 180 -1
SHEET 5 Y 5 ASN l 190 ASP l 192 -1
SHEET 1 Z 3 GLY l 98 THR l 105 0
SHEET 2 Z 3 GLY l 109 ASP l 116 -1
SHEET 3 Z 3 ARG l 121 GLY l 124 -1
SHEET 1 AA 2 TYR l 178 VAL l 180 0
SHEET 2 AA 2 TRP l 185 TYR l 187 -1
SHEET 1 AB 2 VAL l 34 ASN l 38 0
SHEET 2 AB 2 LEU l 41 THR l 44 -1
SHEET 1 AC 5 CYS m 136 GLY m 140 0
SHEET 2 AC 5 THR m 11 ALA m 16 -1
SHEET 3 AC 5 PHE m 20 ASP m 26 -1
SHEET 4 AC 5 GLY m 201 THR m 208 -1
SHEET 5 AC 5 LYS m 214 GLU m 218 -1
SHEET 1 AD 4 ILE m 50 GLY m 56 0
SHEET 2 AD 4 VAL m 107 LEU m 114 -1
SHEET 3 AD 4 GLY m 120 ASP m 126 -1
SHEET 4 AD 4 GLY m 129 GLU m 134 -1
SHEET 1 AE 2 ASN m 29 THR m 31 0
SHEET 2 AE 2 SER m 34 SER m 37 -1
SHEET 1 AF 5 THR n 141 ALA n 143 0
SHEET 2 AF 5 VAL n 11 TYR n 16 -1
SHEET 3 AF 5 GLY n 19 ASP n 25 -1
SHEET 4 AF 5 PHE n 195 ASP n 201 -1
SHEET 5 AF 5 LEU n 206 LYS n 209 -1
SHEET 1 AG 5 LEU n 42 PRO n 44 0
SHEET 2 AG 5 THR n 49 GLY n 55 -1
SHEET 3 AG 5 ASN n 112 VAL n 119 -1
SHEET 4 AG 5 GLN n 125 VAL n 130 -1
SHEET 5 AG 5 THR n 136 SER n 138 -1
SHEET 1 AH 5 ALA A 159 THR A 162 0
SHEET 2 AH 5 SER A 33 ARG A 37 -1
SHEET 3 AH 5 THR A 42 GLN A 47 -1
SHEET 4 AH 5 LEU A 214 THR A 220 -1
SHEET 5 AH 5 LYS A 223 THR A 226 -1
SHEET 1 AI 5 ILE A 63 CYS A 65 0
SHEET 2 AI 5 GLY A 71 ASN A 75 -1
SHEET 3 AI 5 ILE A 131 VAL A 137 -1
SHEET 4 AI 5 PRO A 143 THR A 148 -1
SHEET 5 AI 5 TYR A 154 GLY A 156 -1
SHEET 1 AJ 5 ALA B 161 ILE B 164 0
SHEET 2 AJ 5 SER B 34 LYS B 38 -1
SHEET 3 AJ 5 VAL B 43 GLU B 48 -1
SHEET 4 AJ 5 ILE B 209 ILE B 214 -1
SHEET 5 AJ 5 PHE B 235 LYS B 237 -1
SHEET 1 AK 4 GLY B 72 GLY B 77 0
SHEET 2 AK 4 VAL B 132 GLY B 138 -1
SHEET 3 AK 4 SER B 146 VAL B 150 -1
SHEET 4 AK 4 TYR B 156 PRO B 158 -1
SHEET 1 AL 5 ALA C 161 VAL C 164 0
SHEET 2 AL 5 ALA C 34 MET C 38 -1
SHEET 3 AL 5 GLY C 42 GLU C 48 -1
SHEET 4 AL 5 LEU C 210 ARG C 216 -1
SHEET 5 AL 5 TYR C 225 ILE C 228 -1
SHEET 1 AM 5 TYR C 156 GLY C 158 0
SHEET 2 AM 5 TYR C 145 SER C 150 -1
SHEET 3 AM 5 VAL C 132 TYR C 139 -1
SHEET 4 AM 5 ILE C 72 GLY C 78 -1
SHEET 5 AM 5 LEU C 65 ASN C 69 -1
SHEET 1 AN 5 ALA D 159 GLY D 163 0
SHEET 2 AN 5 CYS D 30 LYS D 35 -1
SHEET 3 AN 5 VAL D 40 GLU D 45 -1
SHEET 4 AN 5 ILE D 208 LYS D 214 -1
SHEET 5 AN 5 ASP D 218 ALA D 221 -1
SHEET 1 AO 5 VAL D 62 LYS D 64 0
SHEET 2 AO 5 VAL D 69 GLY D 75 -1
SHEET 3 AO 5 VAL D 129 PHE D 136 -1
SHEET 4 AO 5 PRO D 143 THR D 148 -1
SHEET 5 AO 5 TYR D 154 SER D 156 -1
SHEET 1 AP 5 ALA E 161 ILE E 164 0
SHEET 2 AP 5 ALA E 29 ILE E 32 -1
SHEET 3 AP 5 VAL E 38 GLU E 43 -1
SHEET 4 AP 5 ALA E 209 THR E 215 -1
SHEET 5 AP 5 GLY E 219 ILE E 222 -1
SHEET 1 AQ 5 PHE E 156 ARG E 158 0
SHEET 2 AQ 5 GLY E 144 ALA E 150 -1
SHEET 3 AQ 5 VAL E 132 ASP E 140 -1
SHEET 4 AQ 5 ILE E 66 GLY E 72 -1
SHEET 5 AQ 5 ILE E 59 ASP E 63 -1
SHEET 1 AR 5 GLY F 157 ILE F 160 0
SHEET 2 AR 5 THR F 34 ARG F 38 -1
SHEET 3 AR 5 HIS F 42 LEU F 48 -1
SHEET 4 AR 5 LEU F 210 GLY F 216 -1
SHEET 5 AR 5 THR F 222 TYR F 224 -1
SHEET 1 AS 4 LEU F 73 GLY F 75 0
SHEET 2 AS 4 VAL F 129 ASP F 137 -1
SHEET 3 AS 4 GLY F 140 PHE F 146 -1
SHEET 4 AS 4 VAL F 152 GLU F 154 -1
SHEET 1 AT 2 ILE F 62 ASP F 66 0
SHEET 2 AT 2 MET F 69 SER F 72 -1
SHEET 1 AU 4 GLY G 158 THR G 161 0
SHEET 2 AU 4 SER G 33 LYS G 37 -1
SHEET 3 AU 4 GLY G 41 LEU G 49 -1
SHEET 4 AU 4 PHE G 208 SER G 216 -1
SHEET 1 AV 5 GLN G 64 VAL G 66 0
SHEET 2 AV 5 ILE G 70 GLY G 76 -1
SHEET 3 AV 5 VAL G 130 ASP G 138 -1
SHEET 4 AV 5 GLY G 141 GLU G 148 -1
SHEET 5 AV 5 SER G 152 GLY G 155 -1
SHEET 1 AW 5 TYR 1 124 ALA 1 127 0
SHEET 2 AW 5 ILE 1 3 THR 1 7 -1
SHEET 3 AW 5 VAL 1 12 ASP 1 17 -1
SHEET 4 AW 5 ILE 1 173 LEU 1 178 -1
SHEET 5 AW 5 VAL 1 183 PHE 1 188 -1
SHEET 1 AX 4 LEU 1 34 ARG 1 36 0
SHEET 2 AX 4 ILE 1 41 SER 1 46 -1
SHEET 3 AX 4 GLY 1 96 ASP 1 103 -1
SHEET 4 AX 4 LYS 1 107 ILE 1 113 -1
SHEET 1 AY 2 THR 1 20 THR 1 22 0
SHEET 2 AY 2 TYR 1 25 ASN 1 28 -1
SHEET 1 AZ 5 TYR 2 124 GLY 2 128 0
SHEET 2 AZ 5 THR 2 2 LYS 2 7 -1
SHEET 3 AZ 5 GLY 2 11 ASP 2 17 -1
SHEET 4 AZ 5 VAL 2 173 GLU 2 179 -1
SHEET 5 AZ 5 ALA 2 184 LEU 2 187 -1
SHEET 1 BA 5 THR 2 119 VAL 2 121 0
SHEET 2 BA 5 GLY 2 107 ILE 2 113 -1
SHEET 3 BA 5 ALA 2 96 ASP 2 104 -1
SHEET 4 BA 5 ILE 2 41 GLY 2 47 -1
SHEET 5 BA 5 LEU 2 34 SER 2 38 -1
SHEET 1 BB 5 PHE 3 135 GLY 3 139 0
SHEET 2 BB 5 ILE 3 10 THR 3 15 -1
SHEET 3 BB 5 VAL 3 20 ASP 3 25 -1
SHEET 4 BB 5 ALA 3 184 LYS 3 190 -1
SHEET 5 BB 5 GLU 3 193 TYR 3 198 -1
SHEET 1 BC 4 ILE 3 42 TYR 3 45 0
SHEET 2 BC 4 VAL 3 48 GLY 3 54 -1
SHEET 3 BC 4 VAL 3 104 ASN 3 112 -1
SHEET 4 BC 4 LYS 3 117 GLY 3 122 -1
SHEET 1 BD 2 LEU 3 28 SER 3 30 0
SHEET 2 BD 2 LEU 3 33 SER 3 36 -1
SHEET 1 BE 5 TYR 4 130 ALA 4 132 0
SHEET 2 BE 5 ILE 4 4 VAL 4 9 -1
SHEET 3 BE 5 SER 4 12 SER 4 18 -1
SHEET 4 BE 5 VAL 4 179 VAL 4 184 -1
SHEET 5 BE 5 ILE 4 189 VAL 4 192 -1
SHEET 1 BF 5 THR 4 124 GLU 4 127 0
SHEET 2 BF 5 LYS 4 113 ASP 4 120 -1
SHEET 3 BF 5 VAL 4 100 ASP 4 108 -1
SHEET 4 BF 5 THR 4 42 GLY 4 48 -1
SHEET 5 BF 5 THR 4 35 SER 4 39 -1
SHEET 1 BG 5 ILE 5 126 VAL 5 129 0
SHEET 2 BG 5 THR 5 3 ARG 5 7 -1
SHEET 3 BG 5 ILE 5 12 VAL 5 16 -1
SHEET 4 BG 5 SER 5 174 THR 5 181 -1
SHEET 5 BG 5 GLY 5 184 ASP 5 192 -1
SHEET 1 BH 3 GLY 5 98 THR 5 105 0
SHEET 2 BH 3 GLY 5 109 ASP 5 116 -1
SHEET 3 BH 3 ARG 5 121 GLY 5 124 -1
SHEET 1 BI 2 VAL 5 34 ASN 5 38 0
SHEET 2 BI 2 LEU 5 41 THR 5 44 -1
SHEET 1 BJ 5 CYS 6 136 GLY 6 140 0
SHEET 2 BJ 5 THR 6 11 ALA 6 16 -1
SHEET 3 BJ 5 ALA 6 21 ASP 6 26 -1
SHEET 4 BJ 5 GLY 6 201 VAL 6 207 -1
SHEET 5 BJ 5 VAL 6 212 GLU 6 218 -1
SHEET 1 BK 4 ILE 6 50 GLY 6 56 0
SHEET 2 BK 4 VAL 6 107 LEU 6 114 -1
SHEET 3 BK 4 GLY 6 120 PHE 6 125 -1
SHEET 4 BK 4 TYR 6 131 ARG 6 133 -1
SHEET 1 BL 2 ASN 6 29 THR 6 31 0
SHEET 2 BL 2 SER 6 34 SER 6 37 -1
SHEET 1 BM 5 THR 7 141 THR 7 144 0
SHEET 2 BM 5 VAL 7 11 LYS 7 15 -1
SHEET 3 BM 5 GLY 7 19 ASP 7 25 -1
SHEET 4 BM 5 PHE 7 195 ASP 7 201 -1
SHEET 5 BM 5 GLY 7 205 LYS 7 209 -1
SHEET 1 BN 4 LEU 7 42 PRO 7 44 0
SHEET 2 BN 4 THR 7 49 GLY 7 55 -1
SHEET 3 BN 4 ASN 7 112 VAL 7 119 -1
SHEET 4 BN 4 GLN 7 125 ASN 7 131 -1
SHEET 1 BO 2 LEU 7 27 TYR 7 30 0
SHEET 2 BO 2 LEU 7 33 ASN 7 37 -1
SHEET 1 BP 2 TYR H 145 ASN H 148 0
SHEET 2 BP 2 LYS H 154 VAL H 157 -1
SHEET 1 BQ 4 GLY H 245 TYR H 249 0
SHEET 2 BQ 4 ILE H 349 THR H 355 1
SHEET 3 BQ 4 CYS H 304 ASP H 309 1
SHEET 4 BQ 4 THR H 270 ILE H 275 1
SHEET 1 BR 2 VAL H 174 VAL H 176 0
SHEET 2 BR 2 ILE H 183 PRO H 186 -1
SHEET 1 BS 4 SER I 146 HIS I 150 0
SHEET 2 BS 4 LEU I 104 ILE I 113 -1
SHEET 3 BS 4 HIS I 117 THR I 121 -1
SHEET 4 BS 4 ASP I 127 SER I 131 -1
SHEET 1 BT 5 ILE I 348 PHE I 350 0
SHEET 2 BT 5 VAL I 219 GLY I 223 1
SHEET 3 BT 5 LYS I 323 ALA I 327 1
SHEET 4 BT 5 SER I 277 ASP I 282 1
SHEET 5 BT 5 THR I 243 VAL I 248 1
SHEET 1 BU 4 MET K 135 HIS K 140 0
SHEET 2 BU 4 LEU K 94 PRO K 102 -1
SHEET 3 BU 4 THR K 107 SER K 111 -1
SHEET 4 BU 4 SER K 117 ARG K 121 -1
SHEET 1 BV 3 ILE K 315 THR K 318 0
SHEET 2 BV 3 GLY K 208 TYR K 212 1
SHEET 3 BV 3 LEU K 334 GLU K 339 1
SHEET 1 BW 2 ALA K 233 VAL K 237 0
SHEET 2 BW 2 SER K 267 ILE K 271 1
SHEET 1 BX 4 ARG L 145 THR L 147 0
SHEET 2 BX 4 ILE L 105 GLU L 111 -1
SHEET 3 BX 4 TYR L 117 ALA L 121 -1
SHEET 4 BX 4 ARG L 126 VAL L 129 -1
SHEET 1 BY 5 ARG L 345 GLU L 348 0
SHEET 2 BY 5 VAL L 218 TYR L 221 1
SHEET 3 BY 5 THR L 321 ALA L 326 1
SHEET 4 BY 5 CYS L 276 ASP L 281 1
SHEET 5 BY 5 ASN L 242 PRO L 247 1
SHEET 1 BZ 5 THR M 126 PRO M 130 0
SHEET 2 BZ 5 ALA M 116 THR M 121 -1
SHEET 3 BZ 5 VAL M 79 VAL M 85 -1
SHEET 4 BZ 5 LEU M 145 VAL M 148 -1
SHEET 5 BZ 5 ILE M 155 THR M 158 -1
SHEET 1 CA 5 ARG M 345 GLU M 348 0
SHEET 2 CA 5 ALA M 218 TYR M 221 1
SHEET 3 CA 5 VAL M 321 ALA M 326 1
SHEET 4 CA 5 THR M 276 ASP M 281 1
SHEET 5 CA 5 PHE M 243 ALA M 247 1
SHEET 1 CB 4 ARG J 112 LEU J 115 0
SHEET 2 CB 4 TYR J 71 VAL J 79 -1
SHEET 3 CB 4 LYS J 83 VAL J 88 -1
SHEET 4 CB 4 LYS J 93 ASP J 97 -1
SHEET 1 CC 5 LYS J 209 VAL J 213 0
SHEET 2 CC 5 SER J 243 ASP J 248 1
SHEET 3 CC 5 ILE J 288 ALA J 293 1
SHEET 4 CC 5 GLY J 184 LEU J 187 1
SHEET 5 CC 5 ILE J 310 ILE J 314 1
LINK OG1 THR H 257 MG MG H 501 1555 1555 1.89
LINK OG1 THR I 230 MG MG I 502 1555 1555 1.80
LINK OG1 THR K 220 MG MG K 502 1555 1555 2.32
LINK OG1 THR L 229 MG MG L 502 1555 1555 2.09
LINK OG1 THR M 229 MG MG M 502 1555 1555 1.77
LINK OG1 THR J 196 MG MG J 502 1555 1555 2.05
LINK MG MG H 501 O2B ATP H 502 1555 1555 2.57
LINK MG MG H 501 O2G ATP H 502 1555 1555 2.59
LINK O2B ATP I 501 MG MG I 502 1555 1555 2.94
LINK O1G ATP K 501 MG MG K 502 1555 1555 1.98
LINK O1B ATP K 501 MG MG K 502 1555 1555 2.90
LINK O2G ATP L 501 MG MG L 502 1555 1555 2.73
LINK O2B ATP L 501 MG MG L 502 1555 1555 2.80
LINK O2G ATP M 501 MG MG M 502 1555 1555 2.71
LINK O1B ATP M 501 MG MG M 502 1555 1555 2.62
LINK O3B ADP J 501 MG MG J 502 1555 1555 2.09
CISPEP 1 HIS H 95 PRO H 96 0 -3.22
CISPEP 2 ASN I 102 PRO I 103 0 -2.39
CISPEP 3 ALA I 275 PRO I 276 0 2.88
CISPEP 4 VAL K 92 PRO K 93 0 -7.55
CISPEP 5 ALA K 265 PRO K 266 0 6.82
CISPEP 6 GLU L 274 PRO L 275 0 -10.31
CISPEP 7 LEU M 75 PRO M 76 0 -7.48
CISPEP 8 ALA M 274 PRO M 275 0 -5.13
CISPEP 9 ALA J 241 PRO J 242 0 6.31
SITE 1 AC1 2 THR H 257 ATP H 502
SITE 1 AC2 14 GLY H 212 GLY H 253 THR H 254 GLY H 255
SITE 2 AC2 14 LYS H 256 THR H 257 LEU H 258 ASN H 356
SITE 3 AC2 14 ALA H 417 ARG H 420 MG H 501 LYS I 214
SITE 4 AC2 14 ARG I 340 ARG I 343
SITE 1 AC3 14 ILE I 184 GLY I 185 GLY I 186 PRO I 225
SITE 2 AC3 14 GLY I 226 THR I 227 GLY I 228 LYS I 229
SITE 3 AC3 14 THR I 230 LEU I 231 ILE I 361 GLY I 389
SITE 4 AC3 14 MG I 502 ARG J 306
SITE 1 AC4 2 THR I 230 ATP I 501
SITE 1 AC5 19 ASP K 173 GLY K 175 GLY K 176 PRO K 215
SITE 2 AC5 19 GLY K 216 THR K 217 GLY K 218 LYS K 219
SITE 3 AC5 19 THR K 220 MET K 221 GLU K 273 ASN K 319
SITE 4 AC5 19 ILE K 352 THR K 355 GLY K 380 ALA K 381
SITE 5 AC5 19 ALA K 384 MG K 502 ARG L 342
SITE 1 AC6 2 THR K 220 ATP K 501
SITE 1 AC7 18 GLY L 182 ILE L 183 GLY L 225 THR L 226
SITE 2 AC7 18 GLY L 227 LYS L 228 THR L 229 LEU L 230
SITE 3 AC7 18 GLU L 282 ASN L 328 ILE L 360 HIS L 364
SITE 4 AC7 18 GLY L 388 ALA L 389 MG L 502 ARG M 213
SITE 5 AC7 18 ARG M 339 ARG M 342
SITE 1 AC8 2 THR L 229 ATP L 501
SITE 1 AC9 12 ARG H 367 ARG H 370 GLY M 184 PRO M 224
SITE 2 AC9 12 GLY M 225 THR M 226 GLY M 227 LYS M 228
SITE 3 AC9 12 THR M 229 LEU M 230 HIS M 364 MG M 502
SITE 1 AD1 2 THR M 229 ATP M 501
SITE 1 AD2 14 MET J 149 VAL J 150 PRO J 191 GLY J 192
SITE 2 AD2 14 THR J 193 GLY J 194 LYS J 195 THR J 196
SITE 3 AD2 14 LEU J 197 ILE J 327 GLY J 355 ALA J 356
SITE 4 AD2 14 LYS J 359 MG J 502
SITE 1 AD3 2 THR J 196 ADP J 501
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
